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Volumn 23, Issue 6, 2004, Pages 1234-1244

Methanoarchaeal sulfolactate dehydrogenase: Prototype of a new family of NADH-dependent enzymes

Author keywords

Coenzyme M; Dehydrogenase; Hyperthermostable; Methanogens; Pro S hydrogen transfer

Indexed keywords

ENZYME; METHANOARCHAEAL SULFOLACTATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 1942471705     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600147     Document Type: Article
Times cited : (17)

References (60)
  • 3
    • 0026685776 scopus 로고
    • Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold
    • Baker PJ, Britton KL, Rice DW, Rob A, Stillman TJ (1992b) Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. J Mol Biol 228: 662-671
    • (1992) J Mol Biol , vol.228 , pp. 662-671
    • Baker, P.J.1    Britton, K.L.2    Rice, D.W.3    Rob, A.4    Stillman, T.J.5
  • 4
    • 0000268861 scopus 로고
    • Calculation of an OMIT map
    • Bhat TN (1988) Calculation of an OMIT map. J Appl Crystallogr 21: 279-281
    • (1988) J Appl Crystallogr , vol.21 , pp. 279-281
    • Bhat, T.N.1
  • 7
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomics correlates of hyperthermostability
    • Cambillau C, Claverie J-M (2000) Structural and genomics correlates of hyperthermostability. J Biol Chem 275: 32383-32386
    • (2000) J Biol Chem , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.-M.2
  • 8
    • 0030824517 scopus 로고    scopus 로고
    • Ribbons
    • Carter CW, Sweet RM (eds). San Diego, CA: Academic Press
    • Carson M (1997) Ribbons. In Methods in Enzymology, Carter CW, Sweet RM (eds) Vol. CCLXXVII, pp 493-505. San Diego, CA: Academic Press
    • (1997) Methods in Enzymology , vol.277 , pp. 493-505
    • Carson, M.1
  • 9
    • 0032762639 scopus 로고    scopus 로고
    • Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
    • Cusa E, Obradors N, Baldomà L, Badìa J, Aguilar J (1999) Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J Bacteriol 181: 7479-7484
    • (1999) J Bacteriol , vol.181 , pp. 7479-7484
    • Cusa, E.1    Obradors, N.2    Baldomà, L.3    Badìa, J.4    Aguilar, J.5
  • 10
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced colouring capabilities
    • Esnouf RM (1997) An extensively modified version of MolScript that includes greatly enhanced colouring capabilities. J Mol Graph 15: 132-134
    • (1997) J Mol Graph , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 11
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multi-wavelength anomalous diffraction methods
    • Carter CW, Sweet RM (eds). San Diego, CA: Academic Press
    • de la Fortelle E, Bricogne G (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multi-wavelength anomalous diffraction methods. In Methods in Enzymology, Carter CW, Sweet RM (eds) Vol. CCLXXV1, pp 472-494. San Diego, CA: Academic Press
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 13
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French GS, Wilson KS (1978) On the treatment of negative intensity observations. Acta Crystallogr A 34: 517-525
    • (1978) Acta Crystallogr A , vol.34 , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 14
    • 0035832782 scopus 로고    scopus 로고
    • The first example of (S)-2-hydroxyacid dehydrogenases catalysing the transfer of the pro-4S hydrogen of NADH are found in the archaea
    • Graupner M, White RH (2001) The first example of (S)-2-hydroxyacid dehydrogenases catalysing the transfer of the pro-4S hydrogen of NADH are found in the archaea. Biochem Biophys Acta 1548: 169-173
    • (2001) Biochem Biophys Acta , vol.1548 , pp. 169-173
    • Graupner, M.1    White, R.H.2
  • 15
    • 0034099657 scopus 로고    scopus 로고
    • Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea
    • Graupner M, Xu H, White RH (2000) Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J Bacteriol 182: 3688-3692
    • (2000) J Bacteriol , vol.182 , pp. 3688-3692
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 16
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • Carter CW, Sweet RM (eds). San Diego, CA: Academic Press
    • Hendrickson WA, Ogata CM (1997) Phase determination from multiwavelength anomalous diffraction measurements. In Methods in Enzymology, Carter CW, Sweet RM (eds) Vol. CCLXXVI, pp 494-523. San Diego, CA: Academic Press
    • (1997) Methods in Enzymology , vol.276 , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 17
    • 77956940478 scopus 로고
    • Lactate dehydrogenase
    • Boyer PD (ed). New York; Academic Press
    • Holbrook JJ, Liljas A, Steindel SJ, Rossmann MG (1975) Lactate dehydrogenase. In The Enzymes, Boyer PD (ed) Vol. XI, pp 191-292. New York; Academic Press
    • (1975) The Enzymes , vol.11 , pp. 191-292
    • Holbrook, J.J.1    Liljas, A.2    Steindel, S.J.3    Rossmann, M.G.4
  • 18
    • 0025273550 scopus 로고
    • Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus
    • Honka E, Fabry S, Niermann T, Palm P, Hensel R (1990) Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. Eur J Biochem 188: 623-632
    • (1990) Eur J Biochem , vol.188 , pp. 623-632
    • Honka, E.1    Fabry, S.2    Niermann, T.3    Palm, P.4    Hensel, R.5
  • 20
    • 17444398048 scopus 로고    scopus 로고
    • Structure-based identification of a novel NTPase from Methanococcus jannaschii
    • Hwang KY, Chung JH, Kim SH, Han YS, Cho Y (1999) Structure-based identification of a novel NTPase from Methanococcus jannaschii. Nat Struct Biol 6: 691-696
    • (1999) Nat Struct Biol , vol.6 , pp. 691-696
    • Hwang, K.Y.1    Chung, J.H.2    Kim, S.H.3    Han, Y.S.4    Cho, Y.5
  • 21
    • 0037459095 scopus 로고    scopus 로고
    • The oligomeric state of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies
    • Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccaï G, Vellieux FMD (2003) The oligomeric state of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. J Mol Biol 326: 859-873
    • (2003) J Mol Biol , vol.326 , pp. 859-873
    • Irimia, A.1    Ebel, C.2    Madern, D.3    Richard, S.B.4    Cosenza, L.W.5    Zaccaï, G.6    Vellieux, F.M.D.7
  • 22
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • Jacrot B, Zaccaï G (1981) Determination of molecular weight by neutron scattering. Biopolymers 20: 2414-2426
    • (1981) Biopolymers , vol.20 , pp. 2414-2426
    • Jacrot, B.1    Zaccaï, G.2
  • 23
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W (1988) Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Crystallogr 21: 916-924
    • (1988) J Appl Crystallogr , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 24
    • 0037052458 scopus 로고    scopus 로고
    • Life and the evolution of earth's atmosphere
    • Kasting JF, Siefert JL (2002) Life and the evolution of earth's atmosphere. Science 296: 1066-1068
    • (2002) Science , vol.296 , pp. 1066-1068
    • Kasting, J.F.1    Siefert, J.L.2
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of structures
    • Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of structures. J Appl Crystallogr 24: 946-950
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 26
  • 27
    • 0033775447 scopus 로고    scopus 로고
    • The putative L-lactate dehydrogenase from Methanoccocus jannaschii is an NADPH-dependent L-malate dehydrogenase
    • Madern D (2000) The putative L-lactate dehydrogenase from Methanoccocus jannaschii is an NADPH-dependent L-malate dehydrogenase. Mol Microbiol 37: 1515-1520
    • (2000) Mol Microbiol , vol.37 , pp. 1515-1520
    • Madern, D.1
  • 28
    • 0036100822 scopus 로고    scopus 로고
    • Molecular evolution within the L-malate and L-lactate dehydrogenase super-family
    • Madern D (2002) Molecular evolution within the L-malate and L-lactate dehydrogenase super-family. J Mol Evol 54: 825-840
    • (2002) J Mol Evol , vol.54 , pp. 825-840
    • Madern, D.1
  • 29
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Carter CW and Sweet RM (eds). San Diego, CA: Academic Press
    • Merritt EA, Bacon DJ (1997) Raster3D photorealistic molecular graphics. In Methods in Enzymology, Carter CW and Sweet RM (eds) Vol. CCLXXVII, pp 505-524. San Diego, CA: Academic Press
    • (1997) Methods in Enzymology , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 30
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr A 50: 157-163
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 33
    • 0002634621 scopus 로고
    • Maximum likelihoo refinement of heavy atom parameters
    • Wolf W, Evans PR, Leslie AGW (eds). Warrington, UK: SERC Daresbury Laboratory
    • Otwinowski Z (1991) Maximum likelihood refinement of heavy atom parameters. In Isomorphous Replacement and Anomalous Scattering, Proceedings of the CCP4 Study Weekend, Wolf W, Evans PR, Leslie AGW (eds) pp 80-86. Warrington, UK: SERC Daresbury Laboratory
    • (1991) Isomorphous Replacement and Anomalous Scattering, Proceedings of the CCP4 Study Weekend , pp. 80-86
    • Otwinowski, Z.1
  • 34
    • 0029853148 scopus 로고    scopus 로고
    • WWW-query: An on line retrieval system for biological sequences data banks
    • Perrière G, Gouy M (1996) WWW-query: an on line retrieval system for biological sequences data banks. Biochimie 78: 364-369
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 35
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo JS (2000) A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal Biochem 279: 151-163
    • (2000) Anal Biochem , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 37
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units
    • Ramakrishnan C, Ramachandran GN, Sasikeharan V (1965) Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units. Biophys J 5: 909-933
    • (1965) Biophys J , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2    Sasikeharan, V.3
  • 38
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read RJ (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42: 140-149
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 39
    • 0034620588 scopus 로고    scopus 로고
    • Halophilic adaptation: Novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui
    • Richard SB, Madern M, Garcin E, Zaccai G (2000) Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry 39: 992-1000
    • (2000) Biochemistry , vol.39 , pp. 992-1000
    • Richard, S.B.1    Madern, M.2    Garcin, E.3    Zaccai, G.4
  • 42
    • 1542563485 scopus 로고
    • Evolution and structural relationships among dehydrogenases
    • Boyer PD (ed). New York: Academic Press
    • Rossmann MG, Liljas A, Brändén C-I, Banaszak LJ (1975) Evolution and structural relationships among dehydrogenases. In The Enzymes, Boyer PD (ed) Vol. XI, pp 61-102. New York: Academic Press
    • (1975) The Enzymes , vol.11 , pp. 61-102
    • Rossmann, M.G.1    Liljas, A.2    Brändén, C.-I.3    Banaszak, L.J.4
  • 44
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78: 1606-1619
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 45
    • 0031002263 scopus 로고    scopus 로고
    • Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga
    • Selig M, Xavier KB, Santos H, Schonheit P (1997) Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga. Arch Microbiol 167: 217-232
    • (1997) Arch Microbiol , vol.167 , pp. 217-232
    • Selig, M.1    Xavier, K.B.2    Santos, H.3    Schonheit, P.4
  • 46
    • 0020712821 scopus 로고
    • NAD-linked L(+) -lactate dehydrogenase from the strict aerobe Alcaligenes eutrophus. 1. Purification and properties
    • Steinbüchel A, Schlegel HG (1983) NAD-linked L(+) -lactate dehydrogenase from the strict aerobe Alcaligenes eutrophus. 1. Purification and properties. Eur J Biochem 130: 321-328
    • (1983) Eur J Biochem , vol.130 , pp. 321-328
    • Steinbüchel, A.1    Schlegel, H.G.2
  • 47
    • 0033066726 scopus 로고    scopus 로고
    • Extremophiles and their adaptation to hot environments
    • Stetter KO (1999) Extremophiles and their adaptation to hot environments. FEBS Lett 452: 22-25
    • (1999) FEBS Lett , vol.452 , pp. 22-25
    • Stetter, K.O.1
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 50
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J Mol Biol 229: 105-124
    • (1993) J Mol Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 52
    • 0001408294 scopus 로고    scopus 로고
    • Computation of Bhat's OMIT maps with different coefficients
    • Vellieux FMD, Dijkstra BW (1997) Computation of Bhat's OMIT maps with different coefficients. J Appl Crystallogr 30: 396-399
    • (1997) J Appl Crystallogr , vol.30 , pp. 396-399
    • Vellieux, F.M.D.1    Dijkstra, B.W.2
  • 53
    • 0030863952 scopus 로고    scopus 로고
    • Noncrystallographic symmetry averaging in phase refinement and extension
    • Carter CW, Sweet RM (eds). San Diego, CA: Academic Press
    • Vellieux FMD, Read RJ (1997) Noncrystallographic symmetry averaging in phase refinement and extension. In Methods in Enzymology, Carter CW, Sweet RM (eds) Vol. CCLXXVII, pp 18-53. San Diego, CA: Academic Press
    • (1997) Methods in Enzymology , vol.277 , pp. 18-53
    • Vellieux, F.M.D.1    Read, R.J.2
  • 54
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65: 1-43
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 56
    • 0034141555 scopus 로고    scopus 로고
    • Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution
    • Wang H, Boisvert D, Kim KK, Kim R, Kim S-H (2000) Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution. EMBO J 19: 317-323
    • (2000) EMBO J , vol.19 , pp. 317-323
    • Wang, H.1    Boisvert, D.2    Kim, K.K.3    Kim, R.4    Kim, S.-H.5
  • 57
    • 0019316535 scopus 로고
    • Structural and functional diversity in 4-alpha-helical proteins
    • Weber PC, Salemme FR (1980) Structural and functional diversity in 4-alpha-helical proteins. Nature 287: 82-84
    • (1980) Nature , vol.287 , pp. 82-84
    • Weber, P.C.1    Salemme, F.R.2
  • 59
    • 0035219754 scopus 로고    scopus 로고
    • Biosynthesis of the methanogenic cofactors
    • White RH (2001) Biosynthesis of the methanogenic cofactors. Vitam Horm 61: 299-337
    • (2001) Vitam Horm , vol.61 , pp. 299-337
    • White, R.H.1
  • 60
    • 33845318295 scopus 로고
    • Interactions of pyrophosphate moieties with α-helices in dinucleotide binding proteins
    • Wierenga RK, De Maeyer MCH, Hol WGJ (1985) Interactions of pyrophosphate moieties with α-helices in dinucleotide binding proteins. Biochemistry 24: 1346-1357
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3


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