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Volumn 1837, Issue 7, 2014, Pages 964-981

Biochemical fossils of the ancient transition from geoenergetics to bioenergetics in prokaryotic one carbon compound metabolism

Author keywords

Acetogens; C1 world; Hydrothermal vents; Methanogens; Origin of life; Pterins

Indexed keywords

ACETYL COENZYME A; CARBON; CARBON DIOXIDE; FERREDOXIN; METHANOPTERIN; METHYL GROUP; TETRAHYDROFOLIC ACID; TETRAHYDROMETHANOPTERIN; THIOESTER; UNCLASSIFIED DRUG;

EID: 84901837899     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.02.001     Document Type: Article
Times cited : (74)

References (227)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • J.P. Abrahams, A.G. Leslie, R. Lutter, and J.E. Walker Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 5
    • 0035093350 scopus 로고    scopus 로고
    • Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria
    • DOI 10.1016/S0168-6445(00)00062-0, PII S0168644500000620
    • J.P. Amend, and E.L. Shock Energetics of overall metabolic reactions of thermophilic and hyperthermophilic archaea and bacteria FEMS Microbiol. Rev. 25 2001 175 243 (Pubitemid 32203705)
    • (2001) FEMS Microbiology Reviews , vol.25 , Issue.2 , pp. 175-243
    • Amend, J.P.1    Shock, E.L.2
  • 6
    • 0037304408 scopus 로고    scopus 로고
    • Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins
    • DOI 10.1016/S1367-5931(02)00018-2
    • V. Anantharaman, L. Aravind, and E.V. Koonin Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins Curr. Opin. Chem. Biol. 7 2003 12 20 (Pubitemid 36126487)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.1 , pp. 12-20
    • Anantharaman, V.1    Aravind, L.2    Koonin, E.V.3
  • 8
    • 84860533432 scopus 로고    scopus 로고
    • Processes on the young earth and the habitats of early life
    • N. Arndt, and E. Nisbet Processes on the young earth and the habitats of early life Annu. Rev. Earth Planet. Sci. 40 2012 521 549
    • (2012) Annu. Rev. Earth Planet. Sci. , vol.40 , pp. 521-549
    • Arndt, N.1    Nisbet, E.2
  • 9
    • 6044276851 scopus 로고    scopus 로고
    • 420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family
    • DOI 10.1016/j.str.2004.02.010, PII S0969212604000528
    • 420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family Structure 12 2004 361 370 (Pubitemid 38353057)
    • (2004) Structure , vol.12 , Issue.3 , pp. 361-370
    • Aufhammer, S.W.1    Warkentin, E.2    Berk, H.3    Shima, S.4    Thauer, R.K.5    Ermler, U.6
  • 11
    • 0034613029 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis 6-hydroxymethyl-7,8- dihydropteroate synthase in complex with pterin monophosphate: New insight into the enzymatic mechanism and sulfa-drug action
    • A.M. Baca, R. Sirawaraporn, S. Turley, W. Sirawaraporn, and W.G. Hol Crystal structure of Mycobacterium tuberculosis 6-hydroxymethyl-7,8- dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action J. Mol. Biol. 302 2000 1193 1212
    • (2000) J. Mol. Biol. , vol.302 , pp. 1193-1212
    • Baca, A.M.1    Sirawaraporn, R.2    Turley, S.3    Sirawaraporn, W.4    Hol, W.G.5
  • 12
    • 0014178256 scopus 로고
    • Inorganic pyrophosphate and the evolution of biological energy transformation
    • H. Baltscheffsky Inorganic pyrophosphate and the evolution of biological energy transformation Acta Chem. Scand. 21 1967 1973 1974
    • (1967) Acta Chem. Scand. , vol.21 , pp. 1973-1974
    • Baltscheffsky, H.1
  • 13
    • 84866048164 scopus 로고    scopus 로고
    • Radical SAM enzymes involved in the biosynthesis of purine-based natural products
    • V. Bandarian Radical SAM enzymes involved in the biosynthesis of purine-based natural products Biochim. Biophys. Acta Proteins Proteomics 1824 2012 1245 1253
    • (2012) Biochim. Biophys. Acta Proteins Proteomics , vol.1824 , pp. 1245-1253
    • Bandarian, V.1
  • 14
    • 0041766196 scopus 로고    scopus 로고
    • 12: Catalysis by cobalamin-dependent enzymes
    • DOI 10.1146/annurev.biochem.72.121801.161828
    • 12: catalysis by cobalamin-dependent enzymes Annu. Rev. Biochem. 72 2003 209 247 (Pubitemid 36930446)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 209-247
    • Banerjee, R.1    Ragsdale, S.W.2
  • 15
    • 0347930814 scopus 로고    scopus 로고
    • Application of a colorimetric assay to identify putative ribofuranosylaminobenzene 5′-phosphate synthase genes expressed with activity in Escherichia coli
    • M.E. Bechard, S. Chhatwal, R.E. Garcia, and M.E. Rasche Application of a colorimetric assay to identify putative ribofuranosylaminobenzene 5′-phosphate synthase genes expressed with activity in Escherichia coli Biol. Proced. Online 5 2003 69 77 (Pubitemid 38097501)
    • (2003) Biological Procedures Online , vol.5 , Issue.1 , pp. 69-77
    • Bechard, M.E.1    Chhatwal, S.2    Garcia, R.E.3    Rasche, M.E.4
  • 19
    • 59949099238 scopus 로고    scopus 로고
    • NMR-derived folate-bound structure of dihydrofolate reductase 1 from the halophile Haloferax volcani
    • A.F.B. Boroujerdi, and J.K. Young NMR-derived folate-bound structure of dihydrofolate reductase 1 from the halophile Haloferax volcani Biopolymers 91 2009 140 144
    • (2009) Biopolymers , vol.91 , pp. 140-144
    • Boroujerdi, A.F.B.1    Young, J.K.2
  • 20
    • 57749185463 scopus 로고    scopus 로고
    • Parallel adaptations to high temperatures in the Archaean eon
    • B. Boussau, S. Blanquart, A. Necsulea, N. Lartillot, and M. Gouy Parallel adaptations to high temperatures in the Archaean eon Nature 456 2008 942 945
    • (2008) Nature , vol.456 , pp. 942-945
    • Boussau, B.1    Blanquart, S.2    Necsulea, A.3    Lartillot, N.4    Gouy, M.5
  • 22
    • 84861138834 scopus 로고    scopus 로고
    • The emergence and early evolution of biological carbon-fixation
    • R. Braakman, and E. Smith The emergence and early evolution of biological carbon-fixation PLoS Comput. Biol. 8 2012 e1002455
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002455
    • Braakman, R.1    Smith, E.2
  • 23
    • 84873333102 scopus 로고    scopus 로고
    • The compositional and evolutionary logic of metabolism
    • R. Braakman, and E. Smith The compositional and evolutionary logic of metabolism Phys. Biol. 10 2013 011001
    • (2013) Phys. Biol. , vol.10 , pp. 011001
    • Braakman, R.1    Smith, E.2
  • 24
    • 0029974924 scopus 로고    scopus 로고
    • A role for pabAB, a p-aminobenzoate synthase gene of Streptomyces venezuelae ISP5230, in chloramphenicol biosynthesis
    • M.P. Brown, K.A. Aidoo, and L.C. Vining A role for pabAB, a p-aminobenzoate synthase gene of Streptomyces venezuelae ISP5230, in chloramphenicol biosynthesis Microbiology 142 1996 1345 1355 (Pubitemid 26193843)
    • (1996) Microbiology , vol.142 , Issue.6 , pp. 1345-1355
    • Brown, M.P.1    Aidoo, K.A.2    Vining, L.C.3
  • 25
    • 6344231741 scopus 로고    scopus 로고
    • Tetrahydrofolate-specific enzymes in Methanosarcina barkeri and growth dependence of this methanogenic archaeon on folic acid or p-aminobenzoic acid
    • DOI 10.1007/s00203-004-0714-0
    • B. Buchenau, and R.K. Thauer Tetrahydrofolate-specific enzymes in Methanosarcina barkeri and growth dependence of this methanogenic archaeon on folic acid or p-aminobenzoic acid Arch. Microbiol. 182 2004 313 325 (Pubitemid 39403206)
    • (2004) Archives of Microbiology , vol.182 , Issue.4 , pp. 313-325
    • Buchenau, B.1    Thauer, R.K.2
  • 29
    • 0032479058 scopus 로고    scopus 로고
    • 1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea
    • DOI 10.1126/science.281.5373.99
    • L. Chistoserdova, J.A. Vorholt, R.K. Thauer, and M.E. Lidstrom C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea Science 281 1998 99 102 (Pubitemid 28354052)
    • (1998) Science , vol.281 , Issue.5373 , pp. 99-102
    • Chistoserdova, L.1    Vorholt, J.A.2    Thauer, R.K.3    Lidstrom, M.E.4
  • 30
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO J. 5 1986 823 826
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 31
    • 0034601917 scopus 로고    scopus 로고
    • 8 barrels: Implications for the evolution of metabolic pathways
    • 8 barrels: implications for the evolution of metabolic pathways J. Mol. Biol. 303 2000 627 640
    • (2000) J. Mol. Biol. , vol.303 , pp. 627-640
    • Copley, R.R.1    Bork, P.2
  • 32
    • 43749088927 scopus 로고    scopus 로고
    • The subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: Functional implications
    • M. Cottevieille, E. Larquet, S. Jonic, M.V. Petoukhov, G. Caprini, S. Paravisi, D.I. Svergun, M.A. Vanoni, and N. Boisset The subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: functional implications J. Biol. Chem. 283 2008 8237 8249
    • (2008) J. Biol. Chem. , vol.283 , pp. 8237-8249
    • Cottevieille, M.1    Larquet, E.2    Jonic, S.3    Petoukhov, M.V.4    Caprini, G.5    Paravisi, S.6    Svergun, D.I.7    Vanoni, M.A.8    Boisset, N.9
  • 35
    • 84869388277 scopus 로고    scopus 로고
    • Comparative genomics guided discovery of two missing archaeal enzyme families involved in the biosynthesis of the pterin moiety of tetrahydromethanopterin and tetrahydrofolate
    • V. de Crécy-Lagard, G. Phillips, L.L. Grochowski, B. El Yacoubi, F. Jenney, M.W.W. Adams, A.G. Murzin, and R.H. White Comparative genomics guided discovery of two missing archaeal enzyme families involved in the biosynthesis of the pterin moiety of tetrahydromethanopterin and tetrahydrofolate ACS Chem. Biol. 7 2012 1807 1816
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1807-1816
    • De Crécy-Lagard, V.1    Phillips, G.2    Grochowski, L.L.3    El Yacoubi, B.4    Jenney, F.5    Adams, M.W.W.6    Murzin, A.G.7    White, R.H.8
  • 38
    • 44449149379 scopus 로고    scopus 로고
    • Life close to the thermodynamic limit: How methanogenic archaea conserve energy
    • U. Deppenmeier, and V. Müller Life close to the thermodynamic limit: how methanogenic archaea conserve energy Results Probl. Cell Differ. 45 2007 121 152
    • (2007) Results Probl. Cell Differ. , vol.45 , pp. 121-152
    • Deppenmeier, U.1    Müller, V.2
  • 39
    • 0014198149 scopus 로고
    • Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization
    • H.W. Dickerman, E. Steers Jr., B.G. Redfield, and H. Weissbach Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization J. Biol. Chem. 242 1967 1522 1525
    • (1967) J. Biol. Chem. , vol.242 , pp. 1522-1525
    • Dickerman, H.W.1    Steers, Jr.E.2    Redfield, B.G.3    Weissbach, H.4
  • 41
    • 37749020557 scopus 로고    scopus 로고
    • An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites
    • S. Dittrich, S.L. Mitchell, A.M. Blagborough, Q. Wang, P. Wang, P.F.G. Sims, and J.E. Hyde An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites Mol. Microbiol. 67 2008 609 618
    • (2008) Mol. Microbiol. , vol.67 , pp. 609-618
    • Dittrich, S.1    Mitchell, S.L.2    Blagborough, A.M.3    Wang, Q.4    Wang, P.5    Sims, P.F.G.6    Hyde, J.E.7
  • 42
    • 0037066711 scopus 로고    scopus 로고
    • Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer
    • DOI 10.1074/jbc.M111877200
    • D. Dobritzsch, S. Ricagno, G. Schneider, K.D. Schnackerz, and Y. Lindqvist Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. implications for mechanism of inhibition and electron transfer J. Biol. Chem. 277 2002 13155 13166 (Pubitemid 34952686)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13155-13166
    • Dobritzsch, D.1    Ricagno, S.2    Schneider, G.3    Schnackerz, K.D.4    Lindqvist, Y.5
  • 43
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl- CoA synthase
    • DOI 10.1126/science.1075843
    • T.I. Doukov, T.M. Iverson, J. Seravalli, S.W. Ragsdale, and C.L. Drennan A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase Science 298 2002 567 572 (Pubitemid 35215305)
    • (2002) Science , vol.298 , Issue.5593 , pp. 567-572
    • Doukov, T.I.1    Iverson, T.M.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 44
    • 4544359293 scopus 로고    scopus 로고
    • Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway
    • DOI 10.1074/jbc.M406442200
    • R.V. Dumitru, and S.W. Ragsdale Mechanism of 4-(beta-D-ribofuranosyl) aminobenzene 5′-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway J. Biol. Chem. 279 2004 39389 39395 (Pubitemid 39258202)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39389-39395
    • Dumitru, R.V.1    Ragsdale, S.W.2
  • 45
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • R.C. Edgar MUSCLE: multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 32 2004 1792 1797 (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 47
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • T.M. Embley, and W. Martin Eukaryotic evolution, changes and challenges Nature 440 2006 623 630
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 48
    • 0030726657 scopus 로고    scopus 로고
    • Crystal structure of methyl-coenzyme M reductase: The key enzyme of biological methane formation
    • DOI 10.1126/science.278.5342.1457
    • U. Ermler, W. Grabarse, S. Shima, M. Goubeaud, and R.K. Thauer Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation Science 278 1997 1457 1462 (Pubitemid 27509817)
    • (1997) Science , vol.278 , Issue.5342 , pp. 1457-1462
    • Ermler, U.1    Grabarse, W.2    Shima, S.3    Goubeaud, M.4    Thauer, R.K.5
  • 50
    • 0038500616 scopus 로고
    • Chemistry of potentially prebiological natural-products
    • A. Eschenmoser, and E. Loewenthal Chemistry of potentially prebiological natural-products Chem. Soc. Rev. 21 1992 1 16
    • (1992) Chem. Soc. Rev. , vol.21 , pp. 1-16
    • Eschenmoser, A.1    Loewenthal, E.2
  • 52
    • 80054087048 scopus 로고    scopus 로고
    • Abiotic methane flux from the Chimaera seep and Tekirova ophiolites (Turkey): Understanding gas exhalation from low temperature serpentinization and implications for Mars
    • G. Etiope, M. Schoell, and H. Hosgormez Abiotic methane flux from the Chimaera seep and Tekirova ophiolites (Turkey): understanding gas exhalation from low temperature serpentinization and implications for Mars Earth Planet. Sci. Lett. 310 2011 96 104
    • (2011) Earth Planet. Sci. Lett. , vol.310 , pp. 96-104
    • Etiope, G.1    Schoell, M.2    Hosgormez, H.3
  • 53
    • 0025284257 scopus 로고
    • The evolution of alpha/beta barrel enzymes
    • G.K. Farber, and G.A. Petsko The evolution of alpha/beta barrel enzymes Trends Biochem. Sci. 15 1990 228 234
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 54
    • 0000122573 scopus 로고
    • Phylogeny Inference Package (version 3.2)
    • J. Felsenstein Phylogeny Inference Package (version 3.2) Cladistics 5 1989 164 166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 55
    • 77957951370 scopus 로고    scopus 로고
    • How to make a living by exhaling methane
    • F.G. Ferry How to make a living by exhaling methane Annu. Rev. Microbiol. 64 2010 453 473
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 453-473
    • Ferry, F.G.1
  • 56
    • 33646873927 scopus 로고    scopus 로고
    • The stepwise evolution of early life driven by energy conservation
    • DOI 10.1093/molbev/msk014
    • J.G. Ferry, and C.H. House The stepwise evolution of early life driven by energy conservation Mol. Biol. Evol. 23 2006 1286 1292 (Pubitemid 43781601)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.6 , pp. 1286-1292
    • Ferry, J.G.1    House, C.H.2
  • 57
    • 44549086610 scopus 로고    scopus 로고
    • 2: Structure and mechanism of riboflavin synthase
    • 2: structure and mechanism of riboflavin synthase Arch. Biochem. Biophys. 474 2008 252 256
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 252-256
    • Fischer, M.1    Bacher, A.2
  • 58
    • 0028989816 scopus 로고
    • Thermoreduction, a hypothesis for the origin of prokaryotes
    • P. Forterre Thermoreduction, a hypothesis for the origin of prokaryotes C. R. Acad. Sci. III 318 1995 415 422
    • (1995) C. R. Acad. Sci. III , vol.318 , pp. 415-422
    • Forterre, P.1
  • 59
    • 24744450331 scopus 로고    scopus 로고
    • The two ages of the RNA world, and the transition to the DNA world: A story of viruses and cells
    • DOI 10.1016/j.biochi.2005.03.015, PII S0300908405000921, Facets of the RNA World
    • P. Forterre The two ages of the RNA world, and the transition to the DNA world: a story of viruses and cells Biochimie 87 2005 793 803 (Pubitemid 41297805)
    • (2005) Biochimie , vol.87 , Issue.9-10 , pp. 793-803
    • Forterre, P.1
  • 60
    • 1842325943 scopus 로고
    • 2 fixation
    • K.H. Schleifer, E. Stackebrandt, FEMS Symposium No. 29 Academic Press London, UK
    • 2 fixation K.H. Schleifer, E. Stackebrandt, Evolution of Prokaryotes FEMS Symposium No. 29 1985 Academic Press London, UK 235 251
    • (1985) Evolution of Prokaryotes , pp. 235-251
    • Fuchs, G.1    Stupperich, E.2
  • 61
    • 80053227684 scopus 로고    scopus 로고
    • Alternative pathways of carbon dioxide fixation: Insights into the early evolution of life?
    • G. Fuchs Alternative pathways of carbon dioxide fixation: insights into the early evolution of life? Annu. Rev. Microbiol. 65 2011 631 658
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 631-658
    • Fuchs, G.1
  • 62
    • 0033534584 scopus 로고    scopus 로고
    • A nonhyperthermophilic common ancestor to extant life forms
    • N. Galtier, N. Tourasse, and M. Gouy A nonhyperthermophilic common ancestor to extant life forms Science 283 1999 220 221
    • (1999) Science , vol.283 , pp. 220-221
    • Galtier, N.1    Tourasse, N.2    Gouy, M.3
  • 63
    • 0345255949 scopus 로고    scopus 로고
    • FolM, A New Chromosomally Encoded Dihydrofolate Reductase in Escherichia coli
    • DOI 10.1128/JB.185.23.7015-7018.2003
    • M. Giladi, N. Altman-Price, I. Levin, L. Levy, and M. Mevarech FolM, a new chromosomally encoded dihydrofolate reductase in Escherichia coli J. Bacteriol. 185 2003 7015 7018 (Pubitemid 37444505)
    • (2003) Journal of Bacteriology , vol.185 , Issue.23 , pp. 7015-7018
    • Giladi, M.1    Altman-Price, N.2    Levin, I.3    Levy, L.4    Mevarech, M.5
  • 65
    • 0036087169 scopus 로고    scopus 로고
    • SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments
    • J. Gough, and C. Chothia Superfamily: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments Nucleic Acids Res. 30 2002 268 272 (Pubitemid 34679561)
    • (2002) Nucleic Acids Research , vol.30 , Issue.1 , pp. 268-272
    • Gough, J.1    Chothia, C.2
  • 66
    • 0033570116 scopus 로고    scopus 로고
    • The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri
    • DOI 10.1016/S0969-2126(00)80059-3
    • W. Grabarse, M. Vaupel, J.A. Vorholt, S. Shima, R.K. Thauer, A. Wittershagen, G. Bourenkov, H.D. Bartunik, and U. Ermler The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri Structure 7 1999 1257 1268 (Pubitemid 29482987)
    • (1999) Structure , vol.7 , Issue.10 , pp. 1257-1268
    • Grabarse, W.1    Vaupel, M.2    Vorholt, J.A.3    Shima, S.4    Thauer, R.K.5    Wittershagen, A.6    Bourenkov, G.7    Bartunik, H.D.8    Ermler, U.9
  • 67
    • 0036005602 scopus 로고    scopus 로고
    • Elucidation of methanogenic coenzyme biosyntheses: From spectroscopy to genomics
    • DOI 10.1039/b103714p
    • D.E. Graham, and R.H. White Elucidation of methanogenic coenzyme biosynthesis: from spectroscopy to genomics Nat. Prod. Rep. 19 2002 133 147 (Pubitemid 34395015)
    • (2002) Natural Product Reports , vol.19 , Issue.2 , pp. 133-147
    • Graham, D.E.1    White, R.H.2
  • 68
    • 0029913246 scopus 로고    scopus 로고
    • Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri
    • DOI 10.1074/jbc.271.14.8352
    • D.A. Grahame, and E. DeMoll Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri J. Biol. Chem. 271 1996 8352 8358 (Pubitemid 26108670)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.14 , pp. 8352-8358
    • Grahame, D.A.1    DeMoll, E.2
  • 69
    • 0026640790 scopus 로고
    • Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme
    • J.M. Green, W.K. Merkel, and B.P. Nichols Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme J. Bacteriol. 174 1992 5317 5323
    • (1992) J. Bacteriol. , vol.174 , pp. 5317-5323
    • Green, J.M.1    Merkel, W.K.2    Nichols, B.P.3
  • 70
    • 34249874032 scopus 로고    scopus 로고
    • 2+-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii
    • DOI 10.1021/bi700052a
    • 2 +-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii Biochemistry 46 2007 6658 6667 (Pubitemid 46870131)
    • (2007) Biochemistry , vol.46 , Issue.22 , pp. 6658-6667
    • Grochowski, L.L.1    Xu, H.2    Leung, K.3    White, R.H.4
  • 72
    • 79958173211 scopus 로고    scopus 로고
    • Biological systems discovery in silico: Radical S-adenosylmethionine protein families and their target peptides for posttranslational modification
    • D.H. Haft, and M.K. Basu Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification J. Bacteriol. 193 2011 2745 2755
    • (2011) J. Bacteriol. , vol.193 , pp. 2745-2755
    • Haft, D.H.1    Basu, M.K.2
  • 73
    • 0041384391 scopus 로고    scopus 로고
    • 420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: A methanogenic enzyme with an unusual quarternary structure
    • DOI 10.1016/S0022-2836(03)00949-5
    • 420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary structure J. Mol. Biol. 332 2003 1047 1057 (Pubitemid 37108798)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.5 , pp. 1047-1057
    • Hagemeier, C.H.1    Shima, S.2    Thauer, R.K.3    Bourenkov, G.4    Bartunik, H.D.5    Ermler, U.6
  • 74
    • 0033947589 scopus 로고    scopus 로고
    • Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1
    • DOI 10.1046/j.1432-1327.2000.01413.x
    • C.H. Hagemeier, L. Chistoserdova, M.E. Lidstrom, R.K. Thauer, and A.J. Vorholt Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 Eur. J. Biochem. 267 2000 3762 3769 (Pubitemid 30423039)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.12 , pp. 3762-3769
    • Hagemeier, C.H.1    Chistoserdova, L.2    Lidstrom, M.E.3    Thauer, R.K.4    Vorholt, J.A.5
  • 75
    • 0036214016 scopus 로고    scopus 로고
    • Posttranscriptional modifications in the A-loop of 23S rRNAs from selected archaea and eubacteria
    • DOI 10.1017/S1355838202013365
    • M.A. Hansen, F. Kirpekar, W. Ritterbusch, and B. Vester Posttranscriptional modifications in the A-loop of 23S rRNAs from selected archaea and eubacteria RNA 8 2002 202 213 (Pubitemid 34288907)
    • (2002) RNA , vol.8 , Issue.2 , pp. 202-213
    • Hansen, M.A.1    Kirpekar, F.2    Ritterbusch, W.3    Vester, B.4
  • 76
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • DOI 10.1073/pnas.0404624101
    • P. Hanzelmann, and H. Schindelin Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans Proc. Natl. Acad. Sci. U. S. A. 101 2004 12870 12875 (Pubitemid 39167550)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.35 , pp. 12870-12875
    • Hanzelmann, P.1    Schindelin, H.2
  • 77
    • 33646468635 scopus 로고    scopus 로고
    • Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
    • P. Hanzelmann, and H. Schindelin Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism Proc. Natl. Acad. Sci. U. S. A. 103 2006 6829 6834
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6829-6834
    • Hanzelmann, P.1    Schindelin, H.2
  • 78
    • 0032504243 scopus 로고    scopus 로고
    • Biosynthesis of pteridines in escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase
    • DOI 10.1074/jbc.273.28.17418
    • C. Haussmann, F. Rohdich, E. Schmidt, A. Bacher, and F. Richter Biosynthesis of pteridines in Escherichia coli - structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase J. Biol. Chem. 273 1998 17418 17424 (Pubitemid 28355070)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17418-17424
    • Haussmann, C.1    Rohdich, F.2    Schmidt, E.3    Bacher, A.4    Richter, G.5
  • 79
    • 0030478259 scopus 로고    scopus 로고
    • Organic sulfur compounds resulting from the interaction of iron sulfide, hydrogen sulfide and carbon dioxide in an anaerobic aqueous environment
    • W. Heinen, and A.M. Lauwers Organic sulfur compounds resulting from the interaction of iron sulfide, hydrogen sulfide and carbon dioxide in an anaerobic aqueous environment Orig. Life Evol. Biosph. 26 1996 131 150
    • (1996) Orig. Life Evol. Biosph. , vol.26 , pp. 131-150
    • Heinen, W.1    Lauwers, A.M.2
  • 80
    • 0000136633 scopus 로고
    • Thermische Erzeugung von Pteridinen und Flavinen aus Aminosä uregemischen
    • B. Heinz, W. Ried, and K. Dose Thermische Erzeugung von Pteridinen und Flavinen aus Aminosäuregemischen Angew. Chem. 91 1979 510 511
    • (1979) Angew. Chem. , vol.91 , pp. 510-511
    • Heinz, B.1    Ried, W.2    Dose, K.3
  • 81
    • 0032066057 scopus 로고    scopus 로고
    • Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus
    • M. Hennig, A. D'Arcy, I.C. Hampele, M.G.P. Page, C. Oefner, and G.E. Dale Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus Nat. Struct. Biol. 5 1998 357 362
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 357-362
    • Hennig, M.1    D'Arcy, A.2    Hampele, I.C.3    Page, M.G.P.4    Oefner, C.5    Dale, G.E.6
  • 82
    • 38649143651 scopus 로고    scopus 로고
    • Energy conservation via electron-transferring flavoprotein in anaerobic bacteria
    • DOI 10.1128/JB.01422-07
    • G. Herrmann, E. Jayamani, G. Mai, and W. Buckel Energy conservation via electron-transferring flavoprotein in anaerobic bacteria J. Bacteriol. 190 2008 784 791 (Pubitemid 351170920)
    • (2008) Journal of Bacteriology , vol.190 , Issue.3 , pp. 784-791
    • Herrmann, G.1    Jayamani, E.2    Mai, G.3    Buckel, W.4
  • 83
    • 0029989411 scopus 로고    scopus 로고
    • The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation
    • A. Hochheimer, D. Linder, R.K. Thauer, and R. Hedderich The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum: structures and transcriptional regulation Eur. J. Biochem. 242 1996 156 162 (Pubitemid 26386367)
    • (1996) European Journal of Biochemistry , vol.242 , Issue.1 , pp. 156-162
    • Hochheimer, A.1    Linder, D.2    Thauer, R.K.3    Hedderich, R.4
  • 84
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 85
    • 84864008626 scopus 로고    scopus 로고
    • Electron bifurcation involved in the energy metabolism of the acetogenic bacterium Moorella thermoacetica growing on glucose or H2 plus CO2
    • H. Huang, S. Wang, J. Moll, and R.K. Thauer Electron bifurcation involved in the energy metabolism of the acetogenic bacterium Moorella thermoacetica growing on glucose or H2 plus CO2 J. Bacteriol. 194 2012 3689 3699
    • (2012) J. Bacteriol. , vol.194 , pp. 3689-3699
    • Huang, H.1    Wang, S.2    Moll, J.3    Thauer, R.K.4
  • 86
    • 0030620774 scopus 로고    scopus 로고
    • Activated acetic acid by carbon fixation on (Fe, Ni)S under primordial conditions
    • C. Huber, and G. Wächtershäuser Activated acetic acid by carbon fixation on (Fe, Ni)S under primordial conditions Science 276 1997 245 247
    • (1997) Science , vol.276 , pp. 245-247
    • Huber, C.1    Wächtershäuser, G.2
  • 87
    • 84862754646 scopus 로고    scopus 로고
    • The archaellum: An old motility structure with a new name
    • K.F. Jarrell, and S.V. Albers The archaellum: an old motility structure with a new name Trends Microbiol. 20 2012 307 312
    • (2012) Trends Microbiol. , vol.20 , pp. 307-312
    • Jarrell, K.F.1    Albers, S.V.2
  • 88
    • 0021847757 scopus 로고
    • Evidence of a common pathway of carbon dioxide reduction to methane in methanogens
    • W.J. Jones, M.I. Donnelly, and R.S. Wolfe Evidence of a common pathway of carbon dioxide reduction to methane in methanogens J. Bacteriol. 163 1985 126 131 (Pubitemid 15011726)
    • (1985) Journal of Bacteriology , vol.163 , Issue.1 , pp. 126-131
    • Jones, W.J.1    Donnelly, M.I.2    Wolfe, R.S.3
  • 89
    • 79952588675 scopus 로고    scopus 로고
    • Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic Archaea
    • A.K. Kaster, J. Moll, K. Parey, and R.K. Thauer Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic Archaea Proc. Natl. Acad. Sci. U. S. A. 108 2011 2981 6298
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2981-6298
    • Kaster, A.K.1    Moll, J.2    Parey, K.3    Thauer, R.K.4
  • 91
    • 67149134671 scopus 로고    scopus 로고
    • On the free energy that drove primordial anabolism
    • M. Kaufmann On the free energy that drove primordial anabolism Int. J. Mol. Sci. 10 2009 1853 1871
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 1853-1871
    • Kaufmann, M.1
  • 92
    • 84874964884 scopus 로고    scopus 로고
    • Archaeal phylogenomics provides evidence in support of a methanogenic origin of the archaea and a thaumarchaeal origin for the eukaryotes
    • S. Kelly, B. Wickstead, and K. Gull Archaeal phylogenomics provides evidence in support of a methanogenic origin of the archaea and a thaumarchaeal origin for the eukaryotes Proc. R. Soc. B 278 2011 1009 1018
    • (2011) Proc. R. Soc. B , vol.278 , pp. 1009-1018
    • Kelly, S.1    Wickstead, B.2    Gull, K.3
  • 93
    • 0020526529 scopus 로고
    • Structural elements of methanopterin, a novel pterin present in Methanobacterium thermoautotrophicum
    • J.T. Keltjens, M.J. Huberts, W.H. Laarhoven, and G.D. Vogels Structural elements of methanopterin, a novel pterin present in Methanobacterium thermoautotrophicum Eur. J. Biochem. 130 1983 537 544 (Pubitemid 13129168)
    • (1983) European Journal of Biochemistry , vol.130 , Issue.3 , pp. 537-544
    • Keltjens, J.T.1    Huberts, M.J.2    Laarhoven, W.H.3    Vogels, G.D.4
  • 94
    • 28244438390 scopus 로고    scopus 로고
    • Recent advances in structural research on ether lipids from archaea including comparative and physiological aspects
    • DOI 10.1271/bbb.69.2019
    • Y. Koga, and H. Morii Recent advances in structural research on ether lipids from archaea including its comparative and physiological aspects Biosci. Biotechnol. Biochem. 69 2005 2019 2034 (Pubitemid 41711822)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.11 , pp. 2019-2034
    • Koga, Y.1    Morii, H.2
  • 95
    • 1542272747 scopus 로고    scopus 로고
    • Comparative genomics, minimal gene-sets and the last universal common ancestor
    • E.V. Koonin Comparative genomics, minimal gene-sets and the last universal common ancestor Nat. Rev. Microbiol. 1 2003 127 136
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 127-136
    • Koonin, E.V.1
  • 96
    • 27844530636 scopus 로고    scopus 로고
    • Natural history of S-adenosylmethionine-binding proteins
    • P.Z. Kozbial, and A.R. Mushegian Natural history of S-adenosylmethionine- binding proteins BMC Struct. Biol. 5 2005 19
    • (2005) BMC Struct. Biol. , vol.5 , pp. 19
    • Kozbial, P.Z.1    Mushegian, A.R.2
  • 97
    • 77950456083 scopus 로고    scopus 로고
    • How did LUCA make a living? Chemiosmosis in the origin of life
    • N. Lane, J.F. Allen, and W. Martin How did LUCA make a living? Chemiosmosis in the origin of life Bioessays 32 2010 271 280
    • (2010) Bioessays , vol.32 , pp. 271-280
    • Lane, N.1    Allen, J.F.2    Martin, W.3
  • 98
    • 84988044805 scopus 로고    scopus 로고
    • The energetics of genome complexity
    • N. Lane, and W. Martin The energetics of genome complexity Nature 467 2010 929 934
    • (2010) Nature , vol.467 , pp. 929-934
    • Lane, N.1    Martin, W.2
  • 99
    • 84871587989 scopus 로고    scopus 로고
    • The origin of membrane bioenergetics
    • N. Lane, and W.F. Martin The origin of membrane bioenergetics Cell 151 2012 1406 1416
    • (2012) Cell , vol.151 , pp. 1406-1416
    • Lane, N.1    Martin, W.F.2
  • 100
    • 72149118443 scopus 로고    scopus 로고
    • Elevated concentrations of formate, acetate and dissolved organic carbon found at the Lost City hydrothermal field
    • S.Q. Lang, D.A. Butterfield, M. Schulte, D.S. Kelley, and M.D. Lilley Elevated concentrations of formate, acetate and dissolved organic carbon found at the Lost City hydrothermal field Geochim. Cosmochim. Acta 74 2010 941 952
    • (2010) Geochim. Cosmochim. Acta , vol.74 , pp. 941-952
    • Lang, S.Q.1    Butterfield, D.A.2    Schulte, M.3    Kelley, D.S.4    Lilley, M.D.5
  • 101
    • 0035860726 scopus 로고    scopus 로고
    • Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor
    • S. Leimkuhler, M.M. Wuebbens, and K.V. Rajagopalan Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor J. Biol. Chem. 276 2001 34695 34701
    • (2001) J. Biol. Chem. , vol.276 , pp. 34695-34701
    • Leimkuhler, S.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 102
    • 0024529940 scopus 로고
    • Structural principles of alpha/beta barrel proteins: The packing of the interior of the sheet
    • A.M. Lesk, C.I. Branden, and C. Chothia Structural principles of alpha/beta barrel proteins: the packing of the interior of the sheet Proteins 5 1989 139 148
    • (1989) Proteins , vol.5 , pp. 139-148
    • Lesk, A.M.1    Branden, C.I.2    Chothia, C.3
  • 103
    • 9644274247 scopus 로고    scopus 로고
    • An alternative pathway for reduced folate biosynthesis in bacteria and halophilic archaea
    • DOI 10.1111/j.1365-2958.2004.04339.x
    • I. Levin, M. Giladi, N. Altman-Price, R. Ortenberg, and M. Mevarech An alternative pathway for reduced folate biosynthesis in bacteria and halophilic archaea Mol. Microbiol. 54 2004 1307 1318 (Pubitemid 39578273)
    • (2004) Molecular Microbiology , vol.54 , Issue.5 , pp. 1307-1318
    • Levin, I.1    Giladi, M.2    Altman-Price, N.3    Ortenberg, R.4    Mevarech, M.5
  • 104
    • 38649099718 scopus 로고    scopus 로고
    • Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri
    • DOI 10.1128/JB.01417-07
    • F. Li, J. Hinderberger, H. Seedorf, J. Zhang, W. Buckel, and R.K. Thauer Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenasee/Etf complex from Clostridium kluyveri J. Bacteriol. 190 2008 843 850 (Pubitemid 351170927)
    • (2008) Journal of Bacteriology , vol.190 , Issue.3 , pp. 843-850
    • Li, F.1    Hinderberger, J.2    Seedorf, H.3    Zhang, J.4    Buckel, W.5    Thauer, R.K.6
  • 105
    • 84862815590 scopus 로고    scopus 로고
    • Methanogens: A window into ancient sulfur metabolism
    • Y. Liu, L.L. Beer, and W.B. Whitman Methanogens: a window into ancient sulfur metabolism Trends Microbiol. 20 2012 251 258
    • (2012) Trends Microbiol. , vol.20 , pp. 251-258
    • Liu, Y.1    Beer, L.L.2    Whitman, W.B.3
  • 106
    • 77957809203 scopus 로고    scopus 로고
    • Cysteine is not the sulfur source for iron-sulfur cluster and methionine biosynthesis in the methanogenic archaeon Methanococcus maripaludis
    • Y. Liu, M. Sieprawska-Lupa, W.B. Whitman, and R.H. White Cysteine is not the sulfur source for iron-sulfur cluster and methionine biosynthesis in the methanogenic archaeon Methanococcus maripaludis J. Biol. Chem. 285 2010 31923 31929
    • (2010) J. Biol. Chem. , vol.285 , pp. 31923-31929
    • Liu, Y.1    Sieprawska-Lupa, M.2    Whitman, W.B.3    White, R.H.4
  • 107
    • 0022526191 scopus 로고
    • The autotrophic pathway of acetate synthesis in acetogenic bacteria
    • L.G. Ljungdahl The autotrophic pathway of acetate synthesis in acetogenic bacteria Annu. Rev. Microbiol. 40 1986 415 450
    • (1986) Annu. Rev. Microbiol. , vol.40 , pp. 415-450
    • Ljungdahl, L.G.1
  • 108
    • 79960572695 scopus 로고    scopus 로고
    • Elucidation of an iterative process of carbon-carbon bond formation of prebiotic significance
    • A. Loison, S. Dubant, P. Adam, and P. Albrecht Elucidation of an iterative process of carbon-carbon bond formation of prebiotic significance Astrobiology 10 2010 973 988
    • (2010) Astrobiology , vol.10 , pp. 973-988
    • Loison, A.1    Dubant, S.2    Adam, P.3    Albrecht, P.4
  • 109
    • 0034664991 scopus 로고    scopus 로고
    • Tetrahydrofolate and tetrahydromethanopterin compared: Functionally distinct carriers in C1 metabolism
    • B.E. Maden Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism Biochem. J. 350 2000 609 629
    • (2000) Biochem. J. , vol.350 , pp. 609-629
    • Maden, B.E.1
  • 110
    • 4644226216 scopus 로고    scopus 로고
    • Abundance of 4Fe-4S motifs in the genomes of methanogens and other prokaryotes
    • DOI 10.1016/j.femsle.2004.08.027, PII S0378109704006287
    • T.A. Major, H. Burd, and W.B. Whitman Abundance of 4Fe-4S motifs in the genomes of methanogens and other prokaryotes FEMS Microbiol. Lett. 239 2004 117 123 (Pubitemid 39296724)
    • (2004) FEMS Microbiology Letters , vol.239 , Issue.1 , pp. 117-123
    • Major, T.A.1    Burd, H.2    Whitman, W.B.3
  • 111
    • 0036708002 scopus 로고    scopus 로고
    • Crystal structures and enzymatic properties of three formyltransferases from archaea: Environmental adaptation and evolutionary relationship
    • DOI 10.1110/ps.0211002
    • B. Mamat, A. Roth, C. Grimm, U. Ermler, C. Tziatzios, D. Schubert, R.K. Thauer, and S. Shima Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship Protein Sci. 11 2002 2168 2178 (Pubitemid 34919620)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2168-2178
    • Mamat, B.1    Roth, A.2    Grimm, C.3    Ermler, U.4    Tziatzios, C.5    Schubert, D.6    Thauer, R.K.7    Shima, S.8
  • 112
    • 46449105488 scopus 로고    scopus 로고
    • Template-directed synthesis of a genetic polymer in a model protocell
    • DOI 10.1038/nature07018, PII NATURE07018
    • S.S. Mansy, J.P. Schrum, M. Krishnamurthy, S. Tobe, D.A. Treco, and J.W. Szostak Template-directed synthesis of a genetic polymer in a model protocell Nature 454 2008 122 125 (Pubitemid 351931971)
    • (2008) Nature , vol.454 , Issue.7200 , pp. 122-125
    • Mansy, S.S.1    Schrum, J.P.2    Krishnamurthy, M.3    Tobe, S.4    Treco, D.A.5    Szostak, J.W.6
  • 114
    • 84857143067 scopus 로고    scopus 로고
    • Hydrogen, metals, bifurcating electrons, and proton gradients: The early evolution of biological energy conservation
    • W.F. Martin Hydrogen, metals, bifurcating electrons, and proton gradients: the early evolution of biological energy conservation FEBS Lett. 586 2012 485 493
    • (2012) FEBS Lett. , vol.586 , pp. 485-493
    • Martin, W.F.1
  • 116
    • 70350059610 scopus 로고    scopus 로고
    • 2 +-dependent cyclic phosphodiesterase catalyzes the hydrolysis of 7,8-dihydro-D-neopterin 2′,3′-cyclic phosphate in methanopterin biosynthesis
    • 2 +-dependent cyclic phosphodiesterase catalyzes the hydrolysis of 7,8-dihydro-D-neopterin 2′,3′-cyclic phosphate in methanopterin biosynthesis Biochemistry 48 2009 9384 9392
    • (2009) Biochemistry , vol.48 , pp. 9384-9392
    • Mashhadi, Z.1    Xu, H.2    White, R.H.3
  • 117
    • 21444443996 scopus 로고    scopus 로고
    • Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy
    • DOI 10.1074/jbc.M413799200
    • M. Mathieu, G. Debousker, S. Vincent, F. Viviani, N. Bamas-Jacques, and V. Mikol Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy J. Biol. Chem. 280 2005 18916 18922 (Pubitemid 41379594)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18916-18922
    • Mathieu, M.1    Debousker, G.2    Vincent, S.3    Viviani, F.4    Bamas-Jacques, N.5    Mikol, V.6
  • 118
    • 0001029771 scopus 로고
    • Providing one-carbon units for biological methylations: Mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase and methyltetrahydrofolate:homocysteine methyltransferase
    • R.G. Matthews, and J.T. Drummond Providing one-carbon units for biological methylations: mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase and methyltetrahydrofolate:homocysteine methyltransferase Chem. Rev. 90 1990 1275 1290
    • (1990) Chem. Rev. , vol.90 , pp. 1275-1290
    • Matthews, R.G.1    Drummond, J.T.2
  • 119
    • 33745303957 scopus 로고    scopus 로고
    • A thermodynamic assessment of energy requirements for biomass synthesis by chemolithoautotrophic micro-organisms in oxic and anoxic environments
    • DOI 10.1111/j.1472-4669.2005.00045.x
    • T.M. McCollom, and J.P. Amend A thermodynamic assessment of energy requirements for biomass synthesis by chemolithoautotrophic microorganisms in oxic and anoxic environments Geology 3 2005 135 144 (Pubitemid 43934447)
    • (2005) Geobiology , vol.3 , Issue.2 , pp. 135-144
    • McCollom, T.M.1    Amend, J.P.2
  • 120
    • 77950489958 scopus 로고    scopus 로고
    • The influence of carbon source on abiotic organic synthesis and carbon isotope fractionation under hydrothermal conditions
    • T.M. McCollom, B.S. Lollar, G. Lacrampe-Couloume, and J.S. Seewald The influence of carbon source on abiotic organic synthesis and carbon isotope fractionation under hydrothermal conditions Geochim. Cosmochim. Acta 74 2010 2717 2740
    • (2010) Geochim. Cosmochim. Acta , vol.74 , pp. 2717-2740
    • McCollom, T.M.1    Lollar, B.S.2    Lacrampe-Couloume, G.3    Seewald, J.S.4
  • 121
    • 84876956988 scopus 로고    scopus 로고
    • Serpentinites, hydrogen, and life
    • T.M. McCollom, and J.S. Seewald Serpentinites, hydrogen, and life Elements 9 2013 129 134
    • (2013) Elements , vol.9 , pp. 129-134
    • McCollom, T.M.1    Seewald, J.S.2
  • 122
    • 84877002789 scopus 로고    scopus 로고
    • Laboratory simulations of abiotic hydrocarbon formation in earth's deep subsurface
    • R.M. Hazen, A.P. Jones, J.A. Baross, Reviews in Mineralogy and Geochemistry
    • T.M. McCollom Laboratory simulations of abiotic hydrocarbon formation in earth's deep subsurface R.M. Hazen, A.P. Jones, J.A. Baross, Carbon in Earth Reviews in Mineralogy and Geochemistry 75 2013 467 794
    • (2013) Carbon in Earth , vol.75 , pp. 467-794
    • McCollom, T.M.1
  • 126
    • 71049187387 scopus 로고    scopus 로고
    • On the origin of life in the Zinc world: I. Photosynthesizing, porous edifices built of hydrothermally precipitated zinc sulfide as cradles of life on Earth
    • A.Y. Mulkidjanian On the origin of life in the Zinc world: I. Photosynthesizing, porous edifices built of hydrothermally precipitated zinc sulfide as cradles of life on Earth Biol. Direct 4 2009 26
    • (2009) Biol. Direct , vol.4 , pp. 26
    • Mulkidjanian, A.Y.1
  • 128
    • 10744223111 scopus 로고    scopus 로고
    • Energy Conservation in Acetogenic Bacteria
    • DOI 10.1128/AEM.69.11.6345-6353.2003
    • V. Müller Energy conservation in acetogenic bacteria Appl. Environ. Microbiol. 69 2003 6345 6353 (Pubitemid 37420162)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.11 , pp. 6345-6353
    • Muller, V.1
  • 129
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • A.G. Murzin, S.E. Brenner, T. Hubbard, and C. Chothia SCOP: a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247 1995 536 540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 130
    • 0032835301 scopus 로고    scopus 로고
    • Barrel structures in proteins: Automatic identification and classification including a sequence analysis of TIM barrels
    • N. Nagano, E.G. Hutchinson, and J.M. Thornton Barrel structures in proteins: automatic identification and classification including a sequence analysis of TIM barrels Protein Sci. 8 1999 2072 2084 (Pubitemid 29489935)
    • (1999) Protein Science , vol.8 , Issue.10 , pp. 2072-2084
    • Nagano, N.1    Hutchinson, E.G.2    Thornton, J.M.3
  • 131
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • N. Nagano, C.A. Orengo, and J.M. Thornton One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions J. Mol. Biol. 321 2002 741 765
    • (2002) J. Mol. Biol. , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 134
    • 38949186487 scopus 로고    scopus 로고
    • The implausibility of metabolic cycles on the prebiotic earth
    • L.E. Orgel The implausibility of metabolic cycles on the prebiotic earth PLoS Biol. 6 2008 e18
    • (2008) PLoS Biol. , vol.6 , pp. 18
    • Orgel, L.E.1
  • 135
    • 0034021158 scopus 로고    scopus 로고
    • The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases
    • DOI 10.1046/j.1365-2958.2000.01815.x
    • R. Ortenberg, O. Rozenblatt-Rosen, and M. Mevarech The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases Mol. Microbiol. 35 2000 1493 1505 (Pubitemid 30175524)
    • (2000) Molecular Microbiology , vol.35 , Issue.6 , pp. 1493-1505
    • Ortenberg, R.1    Rozenblatt-Rosen, O.2    Mevarech, M.3
  • 136
    • 15744402488 scopus 로고    scopus 로고
    • A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5′- monophosphate synthetase: A new enzyme in purine biosynthesis
    • DOI 10.1074/jbc.M413937200
    • K. Ownby, H.M. Xu, and R.H. White A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4-carboxamide-1 β-D-ribofuranosyl 5′-monophosphate synthetase - a new enzyme in purine biosynthesis J. Biol. Chem. 280 2005 10881 10887 (Pubitemid 40418389)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 10881-10887
    • Ownby, K.1    Xu, H.2    White, R.H.3
  • 137
    • 0025901140 scopus 로고
    • Origin of life-facing up to the physical setting
    • N.R. Pace Origin of life-facing up to the physical setting Cell 65 1991 531 533
    • (1991) Cell , vol.65 , pp. 531-533
    • Pace, N.R.1
  • 138
    • 0015268040 scopus 로고
    • The biosynthesis of pteridines. Part VI. Studies of the mechanism of riboflavin biosynthesis
    • T. Paterson, and H.C.S. Wood The biosynthesis of pteridines. Part VI. Studies of the mechanism of riboflavin biosynthesis J. Chem. Soc. Perkin Trans. 1 1972 1051 1056
    • (1972) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1051-1056
    • Paterson, T.1    Wood, H.C.S.2
  • 140
    • 84890043672 scopus 로고    scopus 로고
    • 2 storage
    • 2 storage Science 342 2013 1329 1330
    • (2013) Science , vol.342 , pp. 1329-1330
    • Pereira, I.A.1
  • 141
    • 85021467943 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • M.F. Perutz, J.C. Kendrew, and H.C. Watson The relation between the divergence of sequence and structure in proteins J. Mol. Biol. 13 1965 669 678
    • (1965) J. Mol. Biol. , vol.13 , pp. 669-678
    • Perutz, M.F.1    Kendrew, J.C.2    Watson, H.C.3
  • 142
    • 34548687408 scopus 로고    scopus 로고
    • Early archaean microorganisms preferred elemental sulfur, not sulfate
    • DOI 10.1126/science.1145861
    • P. Philippot, M. Van Zuilen, K. Lepot, C. Thomazo, J. Farquhar, and M.J. Van Kranendonk Early archaean microorganisms preferred elemental sulfur, not sulfate Science 317 2007 1534 1537 (Pubitemid 47422001)
    • (2007) Science , vol.317 , Issue.5844 , pp. 1534-1537
    • Philippot, P.1    Van Zuilen, M.2    Lepot, K.3    Thomazo, C.4    Farquhar, J.5    Van Kranendonk, M.J.6
  • 143
    • 79959287938 scopus 로고    scopus 로고
    • Biosynthesis and function of tRNA modifications in archaea
    • G. Phillips, and V. de Crecy-Lagard Biosynthesis and function of tRNA modifications in archaea Curr. Opin. Microbiol. 14 2011 335 341
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 335-341
    • Phillips, G.1    De Crecy-Lagard, V.2
  • 145
    • 0037134469 scopus 로고    scopus 로고
    • Enzymatic modification of tRNAs. MiaB is an iron-sulfur protein
    • DOI 10.1074/jbc.C100609200
    • F. Pierrel, G.R. Bjork, M. Fontecave, and M. Atta Enzymatic modification of tRNAs - MiaB is an iron-sulfur protein J. Biol. Chem. 277 2002 13367 13370 (Pubitemid 34967927)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13367-13370
    • Pierrel, F.1    Bjork, G.R.2    Fontecave, M.3    Atta, M.4
  • 146
    • 84859090257 scopus 로고    scopus 로고
    • An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis
    • A. Poehlein, S. Schmidt, A.K. Kaster, M. Goenrich, J. Vollmers, and A. Thürmer et al. An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis PLoS One 7 2012 e33439
    • (2012) PLoS One , vol.7 , pp. 33439
    • Poehlein, A.1    Schmidt, S.2    Kaster, A.K.3    Goenrich, M.4    Vollmers, J.5    Thürmer, A.6
  • 147
    • 0034521570 scopus 로고    scopus 로고
    • Methyl-RNA: An evolutionary bridge between RNA and DNA?
    • A. Poole, D. Penny, and B.M. Sjoberg Methyl-RNA: an evolutionary bridge between RNA and DNA? Chem. Biol. 7 2000 R207 R216
    • (2000) Chem. Biol. , vol.7
    • Poole, A.1    Penny, D.2    Sjoberg, B.M.3
  • 148
    • 3242793348 scopus 로고    scopus 로고
    • Two biosynthetic pathways for aromatic amino acids in the archaeon Methanococcus maripaludis
    • DOI 10.1128/JB.186.15.4940-4950.2004
    • I. Porat, B.W. Waters, Q. Teng, and W.B. Whitman Two biosynthetic pathways for aromatic amino acids in the archaeon Methanococcus maripaludis J. Bacteriol. 186 2004 4940 4950 (Pubitemid 38970821)
    • (2004) Journal of Bacteriology , vol.186 , Issue.15 , pp. 4940-4950
    • Porat, I.1    Waters, B.W.2    Teng, Q.3    Whitman, W.B.4
  • 149
    • 67649403399 scopus 로고    scopus 로고
    • 6-Pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria
    • A. Pribat, L. Jeanguenin, A. Lara-Nunez, M.J. Ziemak, J.E. Hyde, V. de Crecy-Lagard, and A.D. Hanson 6-Pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria J. Bacteriol. 191 2009 4158 4165
    • (2009) J. Bacteriol. , vol.191 , pp. 4158-4165
    • Pribat, A.1    Jeanguenin, L.2    Lara-Nunez, A.3    Ziemak, M.J.4    Hyde, J.E.5    De Crecy-Lagard, V.6    Hanson, A.D.7
  • 150
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2 - Approximately maximum-likelihood trees for large alignments
    • M.N. Price, P.S. Dehal, and A.P. Arkin FastTree 2 - approximately maximum-likelihood trees for large alignments PLoS One 5 2010 e9490
    • (2010) PLoS One , vol.5 , pp. 9490
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 152
    • 13444306641 scopus 로고    scopus 로고
    • NCBI reference sequence (RefSeq): A curated non-redundant sequence database of genomes, transcripts and proteins
    • K.D. Pruitt, T. Tatusova, and D.R. Maglott NCBI reference sequence (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins Nucleic Acids Res. 33 2005 D501 D504
    • (2005) Nucleic Acids Res. , vol.33
    • Pruitt, K.D.1    Tatusova, T.2    Maglott, D.R.3
  • 153
    • 34248204828 scopus 로고    scopus 로고
    • Dissimilatory sulfate- and sulfur-reducing prokaryotes
    • M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, E. Stackebrandt, 2nd edn Springer New York, NY
    • R. Rabus, T.A. Hansen, and F. Widdel Dissimilatory sulfate- and sulfur-reducing prokaryotes M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, E. Stackebrandt, 2nd edn The Prokaryotes vol. II 2006 Springer New York, NY 659 768
    • (2006) The Prokaryotes , vol.2 , pp. 659-768
    • Rabus, R.1    Hansen, T.A.2    Widdel, F.3
  • 156
    • 41349119857 scopus 로고    scopus 로고
    • Enzymology of the Wood-Ljungdahl pathway of acetogenesis
    • DOI 10.1196/annals.1419.015, Incredible Anaerobes From Physiology to Genomics to Fuels
    • S.W. Ragsdale Enzymology of the Wood-Ljungdahl pathway of acetogenesis Ann. N. Y. Acad. Sci. 1125 2008 129 136 (Pubitemid 351451161)
    • (2008) Annals of the New York Academy of Sciences , vol.1125 , pp. 129-136
    • Ragsdale, S.W.1
  • 157
    • 0032508349 scopus 로고    scopus 로고
    • Mechanism for the enzymatic formation of 4-(β-D- ribofuranosyl)aminobenzene 5'-phosphate during the biosynthesis of methanopterin
    • DOI 10.1021/bi973086q
    • M.E. Rasche, and R.H. White Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate during the biosynthesis of methanopterin Biochemistry 37 1998 11343 11351 (Pubitemid 28394884)
    • (1998) Biochemistry , vol.37 , Issue.32 , pp. 11343-11351
    • Rasche, M.E.1    White, R.H.2
  • 158
    • 0029137828 scopus 로고
    • The structure and evolution of α/β barrel proteins
    • D. Reardon, and G.K. Farber The structure and evolution of α/β barrel proteins FASEB J. 9 1995 497 503
    • (1995) FASEB J. , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 159
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The european molecular biology open software suite
    • P. Rice, I. Longden, and A. Bleasby EMBOSS: the european molecular biology open software suite Trends Genet. 16 2000 276 277
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 160
    • 0027298448 scopus 로고
    • Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis
    • S.L. Rivers, E. McNairn, F. Blasco, G. Giordano, and D.H. Boxer Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis Mol. Microbiol. 8 1993 1071 1081 (Pubitemid 23187026)
    • (1993) Molecular Microbiology , vol.8 , Issue.6 , pp. 1071-1081
    • Rivers, S.L.1    McNairn, E.2    Blasco, F.3    Giordano, G.4    Boxer, D.H.5
  • 162
    • 0026643934 scopus 로고
    • P-Aminobenzoate synthesis in Escherichia coli: Kinetic and mechanistic characterization of the amidotransferase PabA
    • B. Roux, and C.T. Walsh p-Aminobenzoate synthesis in Escherichia coli: kinetic and mechanistic characterization of the amidotransferase PabA Biochemistry 31 1992 6904 6910
    • (1992) Biochemistry , vol.31 , pp. 6904-6910
    • Roux, B.1    Walsh, C.T.2
  • 163
    • 0028023065 scopus 로고
    • A hydrothermally precipitated catalytic iron sulphide membrane as a first step toward life
    • M.J. Russell, R.M. Daniel, A.J. Hall, and J.A. Sherringham A hydrothermally precipitated catalytic iron sulfide membrane as a first step toward life J. Mol. Evol. 39 1994 231 243 (Pubitemid 24283339)
    • (1994) Journal of Molecular Evolution , vol.39 , Issue.3 , pp. 231-243
    • Russell, M.J.1    Daniel, R.M.2    Hall, A.J.3    Sherringham, J.A.4
  • 164
    • 0030875872 scopus 로고    scopus 로고
    • The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front
    • M.J. Russell, and A.J. Hall The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front J. Geol. Soc. Lond. 154 1997 377 402
    • (1997) J. Geol. Soc. Lond. , vol.154 , pp. 377-402
    • Russell, M.J.1    Hall, A.J.2
  • 165
    • 0002672873 scopus 로고
    • Methionine biosynthesis in Enterobacteriaceae: Biochemical, regulatory, and evolutionary aspects
    • I. Saint-Girons, C. Parsot, M.M. Zakin, O. Bârzu, and G.N. Cohen Methionine biosynthesis in Enterobacteriaceae: biochemical, regulatory, and evolutionary aspects CRC Crit. Rev. Biochem. 23 1988 1 42
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 1-42
    • Saint-Girons, I.1    Parsot, C.2    Zakin, M.M.3    Bârzu, O.4    Cohen, G.N.5
  • 168
    • 77953222884 scopus 로고    scopus 로고
    • The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane
    • S. Scheller, M. Goenrich, R. Boecher, R.K. Thauer, and B. Jaun The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane Nat. Lett. 465 2010 606 609
    • (2010) Nat. Lett. , vol.465 , pp. 606-609
    • Scheller, S.1    Goenrich, M.2    Boecher, R.3    Thauer, R.K.4    Jaun, B.5
  • 170
    • 84890023112 scopus 로고    scopus 로고
    • 2 to formate by a bacterial carbon dioxide reductase
    • 2 to formate by a bacterial carbon dioxide reductase Science 342 2013 1382 1385
    • (2013) Science , vol.342 , pp. 1382-1385
    • Schuchmann, K.1    Muller, V.2
  • 171
    • 33745933654 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis and molybdenum enzymes
    • DOI 10.1146/annurev.arplant.57.032905.105437
    • G. Schwarz, and R.R. Mendel Molybdenum cofactor biosynthesis and molybdenum enzymes Annu. Rev. Plant Biol. 57 2006 623 647 (Pubitemid 44061039)
    • (2006) Annual Review of Plant Biology , vol.57 , pp. 623-647
    • Schwarz, G.1    Mendel, R.R.2
  • 172
    • 0036335358 scopus 로고    scopus 로고
    • Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway
    • DOI 10.1128/JB.184.16.4442-4448.2002
    • J.W. Scott, and M.E. Rasche Purification, overproduction, and partial characterization of beta-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway J. Bacteriol. 184 2002 4442 4448 (Pubitemid 34832572)
    • (2002) Journal of Bacteriology , vol.184 , Issue.16 , pp. 4442-4448
    • Scott, J.W.1    Rasche, M.E.2
  • 173
    • 77957955710 scopus 로고    scopus 로고
    • Mitochondrion-related organelles in eukaryotic protists
    • A.M. Shiflett, and P.J. Johnson Mitochondrion-related organelles in eukaryotic protists Annu. Rev. Microbiol. 64 2010 409 429
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 409-429
    • Shiflett, A.M.1    Johnson, P.J.2
  • 175
    • 0036308360 scopus 로고    scopus 로고
    • Structure and function of enzymes involved in the methanogenic pathway utilizing carbon dioxide and molecular hydrogen
    • S. Shima, E. Warkentin, R.K. Thauer, and U. Ermler Structure and function of enzymes involved in the methanogenic pathway utilizing carbon dioxide and molecular hydrogen J. Biosci. Bioeng. 93 2002 519 530 (Pubitemid 34743648)
    • (2002) Journal of Bioscience and Bioengineering , vol.93 , Issue.6 , pp. 519-530
    • Shima, S.1    Warkentin, E.2    Thauer, R.K.3    Ermler, U.4
  • 176
    • 33244466796 scopus 로고    scopus 로고
    • Comprehensive multigene phylogenies of excavate protists reveal the evolutionary positions of "primitive" eukaryotes
    • DOI 10.1093/molbev/msj068
    • A.G.B. Simpson, Y. Inagaki, and A.J. Roger Comprehensive multigene phylogenies of excavate protists reveal the evolutionary positions of "primitive" eukaryotes Mol. Biol. Evol. 23 2006 615 625 (Pubitemid 43278273)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.3 , pp. 615-625
    • Simpson, A.G.B.1    Inagaki, Y.2    Roger, A.J.3
  • 178
    • 0025602271 scopus 로고
    • An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene
    • J. Slock, D.P. Stahly, C.Y. Han, E.W. Six, and I.P. Crawford An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene J. Bacteriol. 172 1990 7211 7226
    • (1990) J. Bacteriol. , vol.172 , pp. 7211-7226
    • Slock, J.1    Stahly, D.P.2    Han, C.Y.3    Six, E.W.4    Crawford, I.P.5
  • 180
  • 181
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • DOI 10.1016/0168-6445(96)00008-3
    • K.O. Stetter Hyperthermophilic procaryotes FEMS Microbiol. Rev. 18 1996 149 158 (Pubitemid 26186138)
    • (1996) FEMS Microbiology Reviews , vol.18 , Issue.2-3 , pp. 149-158
    • Stetter, K.O.1
  • 184
    • 0030855476 scopus 로고    scopus 로고
    • Prebiotic chemistry: A bioorganic perspective
    • DOI 10.1016/S0040-4020(97)00438-9, PII S0040402097004389
    • J.D. Sutherland, and J.N. Whitfield Prebiotic chemistry: a bioorganic perspective Tetrahedron 53 1998 11493 11527 (Pubitemid 27351434)
    • (1997) Tetrahedron , vol.53 , Issue.34 , pp. 11493-11527
    • Sutherland, J.D.1    Whitfield, J.N.2
  • 186
    • 77951995416 scopus 로고    scopus 로고
    • Folate biosynthesis - Reappraisal of old and novel targets in the search for new antimicrobials
    • J. Swarbrick, P. Iliadesb, J.S. Simpsona, and I. Macreadiec Folate biosynthesis - reappraisal of old and novel targets in the search for new antimicrobials Open Enzyme Inhib. J. 1 2008 12 33
    • (2008) Open Enzyme Inhib. J. , vol.1 , pp. 12-33
    • Swarbrick, J.1    Iliadesb, P.2    Simpsona, J.S.3    Macreadiec, I.4
  • 187
    • 0025750805 scopus 로고
    • Purification and partial characterization of 7,8-dihydro-6- hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100
    • T.L. Talarico, I.K. Dev, W.S. Dallas, R. Ferone, and P.H. Ray Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin- pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100 J. Bacteriol. 173 1991 7029 7032
    • (1991) J. Bacteriol. , vol.173 , pp. 7029-7032
    • Talarico, T.L.1    Dev, I.K.2    Dallas, W.S.3    Ferone, R.4    Ray, P.H.5
  • 188
    • 0026700594 scopus 로고
    • Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
    • T.L. Talarico, P.H. Ray, I.K. Dev, B.M. Merrill, and W.S. Dallas Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase J. Bacteriol. 174 1992 5971 5977
    • (1992) J. Bacteriol. , vol.174 , pp. 5971-5977
    • Talarico, T.L.1    Ray, P.H.2    Dev, I.K.3    Merrill, B.M.4    Dallas, W.S.5
  • 190
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • R.K. Thauer, K. Jungermann, and K. Decker Energy conservation in chemotrophic anaerobic bacteria Bacteriol. Rev. 41 1977 100 180 (Pubitemid 8082287)
    • (1977) Bacteriological Reviews , vol.41 , Issue.1 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 192
    • 37249062588 scopus 로고    scopus 로고
    • A fifth pathway of carbon fixation
    • DOI 10.1126/science.1152209
    • R.K. Thauer A fifth pathway of carbon fixation Science 318 2007 1732 1733 (Pubitemid 350274373)
    • (2007) Science , vol.318 , Issue.5857 , pp. 1732-1733
    • Thauer, R.K.1
  • 193
    • 33645309348 scopus 로고    scopus 로고
    • Evidence from fluid inclusions for microbial methanogenesis in the early Archaean era
    • Y. Ueno, K. Yamada, N. Yoshida, S. Maruyama, and Y. Isozaki Evidence from fluid inclusions for microbial methanogenesis in the early Archaean era Nature 440 2006 516 519
    • (2006) Nature , vol.440 , pp. 516-519
    • Ueno, Y.1    Yamada, K.2    Yoshida, N.3    Maruyama, S.4    Isozaki, Y.5
  • 194
    • 33947380915 scopus 로고    scopus 로고
    • Adaptations to energy stress dictate the ecology and evolution of the Archaea
    • DOI 10.1038/nrmicro1619, PII NRMICRO1619
    • D.L. Valentine Adaptations to energy stress dictate the ecology and evolution of the archaea Nat. Rev. Microbiol. 5 2007 316 323 (Pubitemid 46443608)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.4 , pp. 316-323
    • Valentine, D.L.1
  • 195
    • 65849420352 scopus 로고    scopus 로고
    • Hydrogenosomes and mitosomes: Conservation and evolution of functions
    • M. van der Giezen Hydrogenosomes and mitosomes: conservation and evolution of functions J. Eukaryot. Microbiol. 56 2009 221 231
    • (2009) J. Eukaryot. Microbiol. , vol.56 , pp. 221-231
    • Van Der Giezen, M.1
  • 196
    • 84929718232 scopus 로고
    • Pyrite formation, the first energy source for life - A hypothesis
    • G. Wächtershäuser Pyrite formation, the first energy source for life - a hypothesis Syst. Appl. Microbiol. 10 1988 207 210
    • (1988) Syst. Appl. Microbiol. , vol.10 , pp. 207-210
    • Wächtershäuser, G.1
  • 198
    • 70349577764 scopus 로고    scopus 로고
    • Many nonuniversal archaeal ribosomal proteins are found in conserved gene clusters
    • J. Wang, I. Dasgupta, and G.E. Fox Many nonuniversal archaeal ribosomal proteins are found in conserved gene clusters Archaea 2 2009 241 251
    • (2009) Archaea , vol.2 , pp. 241-251
    • Wang, J.1    Dasgupta, I.2    Fox, G.E.3
  • 199
    • 34848833475 scopus 로고    scopus 로고
    • Elucidating biosynthetic pathways for vitamins and cofactors
    • DOI 10.1039/b703105j
    • M.E. Webb, A. Marquet, R.R. Mendel, F. Rébeillé, and A.G. Smith Elucidating biosynthetic pathways for vitamins and cofactors Nat. Prod. Rep. 24 2007 988 1008 (Pubitemid 47493397)
    • (2007) Natural Product Reports , vol.24 , Issue.5 , pp. 988-1008
    • Webb, M.E.1    Marquet, A.2    Mendel, R.R.3    Rebeille, F.4    Smith, A.G.5
  • 200
    • 34247622409 scopus 로고    scopus 로고
    • Characterization of the role of para-aminobenzoic acid biosynthesis in folate production by Lactococcus lactis
    • DOI 10.1128/AEM.02174-06
    • A. Wegkamp, W. van Oorschot, W.M. de Vos, and E.J. Smid Characterization of the role of para-aminobenzoic acid biosynthesis in folate production by Lactococcus lactis Appl. Environ. Microbiol. 73 2007 2673 2681 (Pubitemid 46668761)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.8 , pp. 2673-2681
    • Wegkamp, A.1    Van Oorschot, W.2    De Vos, W.M.3    Smid, E.J.4
  • 201
    • 0022456467 scopus 로고
    • Biosynthesis of the 7-methylated pterin of methanopterin
    • R.H. White Biosynthesis of the 7-methylated pterin of methanopterin J. Bacteriol. 165 1986 215 218 (Pubitemid 16016065)
    • (1986) Journal of Bacteriology , vol.165 , Issue.1 , pp. 215-218
    • White, R.H.1
  • 202
    • 0024094995 scopus 로고
    • Analysis and characterization of the folates in the nonmethanogenic archaebacteria
    • R.H. White Analysis and characterization of the folates in the nonmethanogenic archaebacteria J. Bacteriol. 170 1988 4608 4612
    • (1988) J. Bacteriol. , vol.170 , pp. 4608-4612
    • White, R.H.1
  • 203
    • 0025341266 scopus 로고
    • Biosynthesis of methanopterin
    • DOI 10.1021/bi00474a027
    • R.H. White Biosynthesis of methanopterin Biochemistry 29 1990 5397 5404 (Pubitemid 20193949)
    • (1990) Biochemistry , vol.29 , Issue.22 , pp. 5397-5404
    • White, R.H.1
  • 204
    • 0026029043 scopus 로고
    • Distribution of folates and modified folates in extremely thermophilic bacteria
    • R.H. White Distribution of folates and modified folates in extremely thermophilic bacteria J. Bacteriol. 173 1991 1987 1991
    • (1991) J. Bacteriol. , vol.173 , pp. 1987-1991
    • White, R.H.1
  • 205
    • 0029923835 scopus 로고    scopus 로고
    • Biosynthesis of methanopterin
    • DOI 10.1021/bi952308m
    • R.H. White Biosynthesis of methanopterin Biochemistry 35 1996 3447 3456 (Pubitemid 26092565)
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3447-3456
    • White, R.H.1
  • 206
    • 0031017062 scopus 로고    scopus 로고
    • Occurrence and biosynthesis of 5-aminoimidazole-4-carboxamide ribonucleotide and N-(β-D-ribofuranosyl)formamide 5'-phosphate in Methanobacterium thermoautotrophicum ΔH
    • R.H. White Occurrence and biosynthesis of 5-aminoimidazole-4-carboxamide ribonucleotide and N-(β-D-ribofuranosyl)formamide 5′-phosphate in Methanobacterium thermoautotrophicum delta(H) J. Bacteriol. 179 1997 563 566 (Pubitemid 27030414)
    • (1997) Journal of Bacteriology , vol.179 , Issue.2 , pp. 563-566
    • White, R.H.1
  • 207
    • 0030925484 scopus 로고    scopus 로고
    • Purine biosynthesis in the domain Archaea without folates or modified folates
    • R.H. White Purine biosynthesis in the domain archaea without folates or modified folates J. Bacteriol. 179 1997 3374 3377 (Pubitemid 27203020)
    • (1997) Journal of Bacteriology , vol.179 , Issue.10 , pp. 3374-3377
    • White, R.H.1
  • 208
    • 0030842549 scopus 로고    scopus 로고
    • Structural characterization of modified folates in archaea
    • R.H. White Structural characterization of modified folates in archaea Vitam. Coenzymes K 281 1997 391 401
    • (1997) Vitam. Coenzymes K , vol.281 , pp. 391-401
    • White, R.H.1
  • 209
    • 0032502820 scopus 로고    scopus 로고
    • Methanopterin biosynthesis: Methylation of the biosynthetic intermediates
    • DOI 10.1016/S0304-4165(97)00148-7, PII S0304416597001487
    • R.H. White Methanopterin biosynthesis: methylation of the biosynthetic intermediates Biochim. Biophys. Acta 1380 1998 257 267 (Pubitemid 28177557)
    • (1998) Biochimica et Biophysica Acta - General Subjects , vol.1380 , Issue.2 , pp. 257-267
    • White, R.H.1
  • 210
    • 0035219754 scopus 로고    scopus 로고
    • Biosynthesis of the methanogenic cofactors
    • PII S0083672901610100
    • R.H. White Biosynthesis of the methanogenic cofactors Vitam. Horm. 61 2001 299 337 (Pubitemid 33805699)
    • (2001) Vitamins and Hormones , vol.61 , pp. 299-337
    • White, R.H.1
  • 211
    • 0345258439 scopus 로고    scopus 로고
    • The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii
    • DOI 10.1016/j.bbagen.2003.09.005
    • R.H. White The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii Biochim. Biophys. Acta 1624 2003 46 53 (Pubitemid 37464940)
    • (2003) Biochimica et Biophysica Acta - General Subjects , vol.1624 , Issue.1-3 , pp. 46-53
    • White, R.H.1
  • 212
    • 79959942911 scopus 로고    scopus 로고
    • The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-d-ribitol moiety in methanopterin
    • R.H. White The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-d-ribitol moiety in methanopterin Biochemistry 50 2011 6041 6052
    • (2011) Biochemistry , vol.50 , pp. 6041-6052
    • White, R.H.1
  • 213
    • 0035896377 scopus 로고    scopus 로고
    • The TIM-barrel fold: A versatile framework for efficient enzymes
    • DOI 10.1016/S0014-5793(01)02236-0, PII S0014579301022360
    • R.K. Wierenga The TIM-barrel fold: a versatile framework for efficient enzymes FEBS Lett. 492 2001 193 198 (Pubitemid 32217827)
    • (2001) FEBS Letters , vol.492 , Issue.3 , pp. 193-198
    • Wierenga, R.K.1
  • 214
    • 78650107466 scopus 로고    scopus 로고
    • Functional analysis of molybdopterin biosynthesis in mycobacteria identifies a fused molybdopterin synthase in Mycobacterium tuberculosis
    • M.J. Williams, B.D. Kana, and V. Mizrahi Functional analysis of molybdopterin biosynthesis in mycobacteria identifies a fused molybdopterin synthase in Mycobacterium tuberculosis J. Bacteriol. 193 2011 98 106
    • (2011) J. Bacteriol. , vol.193 , pp. 98-106
    • Williams, M.J.1    Kana, B.D.2    Mizrahi, V.3
  • 215
    • 84890355580 scopus 로고    scopus 로고
    • An archaeal origin of eukaryotes supports only two primary domains of life
    • T.A. Williams, P.G. Foster, C.J. Cox, and T.M. Embley An archaeal origin of eukaryotes supports only two primary domains of life Nature 504 2013 231 236
    • (2013) Nature , vol.504 , pp. 231-236
    • Williams, T.A.1    Foster, P.G.2    Cox, C.J.3    Embley, T.M.4
  • 217
    • 0017749245 scopus 로고
    • The concept of cellular evolution
    • DOI 10.1007/BF01796132
    • C.R. Woese, and G.E. Fox The concept of cellular evolution J. Mol. Evol. 10 1977 1 6 (Pubitemid 8177803)
    • (1977) Journal of Molecular Evolution , vol.10 , Issue.1 , pp. 1-6
    • Woese, C.R.1    Fox, G.E.2
  • 218
    • 0023184331 scopus 로고
    • Bacterial evolution
    • C.R. Woese Bacterial evolution Microbiol. Rev. 51 1987 221 271 (Pubitemid 17082512)
    • (1987) Microbiological Reviews , vol.51 , Issue.2 , pp. 221-271
    • Woese, C.R.1
  • 220
    • 0032775448 scopus 로고    scopus 로고
    • Identifying two ancient enzymes in Archaea using predicted secondary structure alignment
    • DOI 10.1038/11525
    • H.M. Xu, R. Aurora, G.D. Rose, and R.H. White Identifying two ancient enzymes in archaea using predicted secondary structure alignment Nat. Struct. Biol. 6 1999 750 754 (Pubitemid 29360236)
    • (1999) Nature Structural Biology , vol.6 , Issue.8 , pp. 750-754
    • Xu, H.1    Aurora, R.2    Rose, G.D.3    White, R.H.4
  • 222
    • 0017139089 scopus 로고
    • Characteristics of guanosine triphosphate cyclohydrolase-I purified from Escherichia coli
    • J.J. Yim, and G.M. Brown Characteristics of guanosine triphosphate cyclohydrolase-I purified from Escherichia coli J. Biol. Chem. 251 1976 5087 5094
    • (1976) J. Biol. Chem. , vol.251 , pp. 5087-5094
    • Yim, J.J.1    Brown, G.M.2
  • 223
    • 0035900982 scopus 로고    scopus 로고
    • Metal ion inhibition of nonenzymatic pyridoxal phosphate catalyzed decarboxylation and transamination
    • DOI 10.1021/ja0026354
    • R.F. Zabinski, and M.D. Toney Metal ion inhibition of nonenzymatic pyridoxal phosphate catalyzed decarboxylation and transamination J. Am. Chem. Soc. 123 2001 193 198 (Pubitemid 32062162)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.2 , pp. 193-198
    • Zabinski, R.F.1    Toney, M.D.2
  • 224
    • 0001851807 scopus 로고    scopus 로고
    • Biosynthesis of purine nucleotides
    • F.C. Neidhardt, ASM Press Washington DC
    • H. Zalkin, and P. Nygaard Biosynthesis of purine nucleotides F.C. Neidhardt, Escherichia coli and Salmonella vol. I 1996 ASM Press Washington DC 561 579
    • (1996) Escherichia Coli and Salmonella , vol.1 , pp. 561-579
    • Zalkin, H.1    Nygaard, P.2
  • 226
    • 84857922587 scopus 로고    scopus 로고
    • A novel mechanism of energetic coupling in anaerobes
    • R.K. Thauer A novel mechanism of energetic coupling in anaerobes Environmental Microbiology Reports 3 2011 24 25
    • (2011) Environmental Microbiology Reports , vol.3 , pp. 24-25
    • Thauer, R.K.1
  • 227
    • 28444444163 scopus 로고    scopus 로고
    • 8-barrel enzyme fold
    • DOI 10.1021/cr030191z
    • R. Sterner, and B. Hocker Versatility, stability, and evolution of the (b/a)8-barrel enzyme fold Chem. Rev. 105 2005 4038 4055 (Pubitemid 41724068)
    • (2005) Chemical Reviews , vol.105 , Issue.11 , pp. 4038-4055
    • Sterner, R.1    Hocker, B.2


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