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Volumn 44, Issue 3, 2016, Pages 961-971

Nothing of chemistry disappears in biology': The Top 30 damage-prone endogenous metabolites

Author keywords

Computational biochemistry; Metabolite damage; Metabolome; Side product; Sidereaction; Spontaneous chemistry

Indexed keywords

2 DEOXYRIBONIC ACID; CARBAMOYL PHOSPHATE; ENZYME; GLUTATHIONE; RIBOFLAVIN; S SUCCINYLGLUTATHIONE; THIAMIN DIPHOSPHATE; THIAMINE; UNCLASSIFIED DRUG; AMINO ACID; ANTIOXIDANT; CARBOHYDRATE; NUCLEIC ACID; PROTEIN; THIOL DERIVATIVE; VITAMIN;

EID: 85009754203     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20160073     Document Type: Review
Times cited : (72)

References (61)
  • 1
    • 63549149085 scopus 로고    scopus 로고
    • How could the Gompertz-Makeham law evolve
    • CrossRef PubMed
    • Golubev, A. (2009) How could the Gompertz-Makeham law evolve. J. Theor. Biol. 258, 1-17 CrossRef PubMed.
    • (2009) J. Theor. Biol. , vol.258 , pp. 1-17
    • Golubev, A.1
  • 2
    • 0030277436 scopus 로고    scopus 로고
    • The other side of metabolism: A review
    • Golubev, A.G. (1996) The other side of metabolism: a review. Biochemistry (Mosc.) 61, 2018-2039.
    • (1996) Biochemistry (Mosc.) , vol.61 , pp. 2018-2039
    • Golubev, A.G.1
  • 3
    • 84921468648 scopus 로고    scopus 로고
    • The widespread role of non-enzymatic reactions in cellular metabolism
    • CrossRef PubMed
    • Keller, M.A., Piedrafita, G. and Ralser, M. (2015) The widespread role of non-enzymatic reactions in cellular metabolism. Curr. Opin. Biotechnol. 34, 153-161 CrossRef PubMed.
    • (2015) Curr. Opin. Biotechnol. , vol.34 , pp. 153-161
    • Keller, M.A.1    Piedrafita, G.2    Ralser, M.3
  • 4
    • 84872715396 scopus 로고    scopus 로고
    • Metabolite damage and its repair or pre-emption
    • CrossRef PubMed
    • Linster, C.L., Van Schaftingen, E. and Hanson, A.D. (2013) Metabolite damage and its repair or pre-emption. Nat. Chem. Biol. 9, 72-80 CrossRef PubMed.
    • (2013) Nat. Chem. Biol , vol.9 , pp. 72-80
    • Linster, C.L.1    Van Schaftingen, E.2    Hanson, A.D.3
  • 6
    • 84934300609 scopus 로고    scopus 로고
    • Chemical reactivity drives spatiotemporal organisation of bacterial metabolism
    • de Lorenzo, V., Sekowska, A. and Danchin, A. (2014) Chemical reactivity drives spatiotemporal organisation of bacterial metabolism. FEMS Microbiol. Rev. 2014, 1-29.
    • (2014) FEMS Microbiol. Rev. 2014 , pp. 1-29
    • De Lorenzo, V.1    Sekowska, A.2    Danchin, A.3
  • 7
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • CrossRef PubMed
    • Khersonsky, O. and Tawfik, D.S. (2010) Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471-505 CrossRef PubMed.
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 8
    • 84921613786 scopus 로고    scopus 로고
    • An evolutionary biochemist's perspective on promiscuity
    • CrossRef PubMed
    • Copley, S.D. (2015) An evolutionary biochemist's perspective on promiscuity. Trends Biochem. Sci. 40, 72-78 CrossRef PubMed.
    • (2015) Trends Biochem. Sci , vol.40 , pp. 72-78
    • Copley, S.D.1
  • 9
    • 77954237941 scopus 로고    scopus 로고
    • Homocysteine methyltransferases Mht1 and Sam4 prevent the accumulation of age-damaged (R, S)-AdoMet in the yeast Saccharomyces cerevisiae
    • CrossRef PubMed
    • Vinci, C.R. and Clarke, S.G. (2010) Homocysteine methyltransferases Mht1 and Sam4 prevent the accumulation of age-damaged (R, S)-AdoMet in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 285, 20526-20531 CrossRef PubMed.
    • (2010) J. Biol. Chem , vol.285 , pp. 20526-20531
    • Vinci, C.R.1    Clarke, S.G.2
  • 11
    • 84861422324 scopus 로고    scopus 로고
    • Rethinking glycolysis: On the biochemical logic of metabolic pathways
    • CrossRef PubMed
    • Bar-Even, A., Flamholz, A., Noor, E. and Milo, R. (2012) Rethinking glycolysis: on the biochemical logic of metabolic pathways. Nat. Chem. Biol. 8, 509-517 CrossRef PubMed.
    • (2012) Nat. Chem. Biol , vol.8 , pp. 509-517
    • Bar-Even, A.1    Flamholz, A.2    Noor, E.3    Milo, R.4
  • 14
    • 35148889024 scopus 로고    scopus 로고
    • Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity
    • CrossRef PubMed
    • Withers, S.T., Gottlieb, S.S., Lieu, B., Newman, J.D. and Keasling, J.D. (2007) Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity. Appl. Environ. Microbiol. 73, 6277-6283 CrossRef PubMed.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 6277-6283
    • Withers, S.T.1    Gottlieb, S.S.2    Lieu, B.3    Newman, J.D.4    Keasling, J.D.5
  • 15
    • 79959898098 scopus 로고    scopus 로고
    • Extending biochemical databases by metabolomic surveys
    • CrossRef PubMed
    • Fiehn, O., Barupal, D.K. and Kind, T. (2011) Extending biochemical databases by metabolomic surveys. J. Biol. Chem. 286, 23637-23643 CrossRef PubMed.
    • (2011) J. Biol. Chem , vol.286 , pp. 23637-23643
    • Fiehn, O.1    Barupal, D.K.2    Kind, T.3
  • 16
    • 84893820176 scopus 로고    scopus 로고
    • Reactive carbonyl species in vivo: Generation and dual biological effects
    • CrossRef
    • Semchyshyn, H.M. (2014) Reactive carbonyl species in vivo: generation and dual biological effects. Sci. World J. 2014, 417842 CrossRef.
    • (2014) Sci. World J. , vol.2014 , pp. 417842
    • Semchyshyn, H.M.1
  • 17
    • 0005702150 scopus 로고
    • The mechanism of the enzymatic cleavage of S-adenosylmethionine to α-amino-γ -butyrolactone
    • PubMed
    • Mudd, S.H. (1959) The mechanism of the enzymatic cleavage of S-adenosylmethionine to α-amino-γ -butyrolactone. J. Biol. Chem. 234, 1784-1786 PubMed.
    • (1959) J. Biol. Chem , vol.234 , pp. 1784-1786
    • Mudd, S.H.1
  • 18
    • 84855946759 scopus 로고    scopus 로고
    • Compound toxicity screening and structure-activity relationship modeling in Escherichia coli
    • CrossRef PubMed
    • Planson, A.G., Carbonell, P., Paillard, E., Pollet, N. and Faulon, J.L. (2012) Compound toxicity screening and structure-activity relationship modeling in Escherichia coli. Biotechnol. Bioeng. 109, 846-850 CrossRef PubMed.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 846-850
    • Planson, A.G.1    Carbonell, P.2    Paillard, E.3    Pollet, N.4    Faulon, J.L.5
  • 19
    • 34250836437 scopus 로고    scopus 로고
    • Estimation of Ková ts retention indices using group contributions
    • CrossRef PubMed
    • Stein, S.E., Babushok, V.I., Brown, R.L. and Linstrom, P.J. (2007) Estimation of Ková ts retention indices using group contributions. J. Chem. Inf. Model. 47, 975-980 CrossRef PubMed.
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 975-980
    • Stein, S.E.1    Babushok, V.I.2    Brown, R.L.3    Linstrom, P.J.4
  • 20
    • 51049107514 scopus 로고    scopus 로고
    • Group contribution method for thermodynamic analysis of complex metabolic networks
    • CrossRef PubMed
    • Jankowski, M.D., Henry, C.S., Broadbelt, L.J. and Hatzimanikatis, V. (2008) Group contribution method for thermodynamic analysis of complex metabolic networks. Biophys. J. 95, 1487-1499 CrossRef PubMed.
    • (2008) Biophys. J. , vol.95 , pp. 1487-1499
    • Jankowski, M.D.1    Henry, C.S.2    Broadbelt, L.J.3    Hatzimanikatis, V.4
  • 22
    • 77953578214 scopus 로고    scopus 로고
    • Discovery and analysis of novel metabolic pathways for the biosynthesis of industrial chemicals: 3-hydroxypropanoate
    • PubMed
    • Henry, C.S., Broadbelt, L.J. and Hatzimanikatis, V. (2010) Discovery and analysis of novel metabolic pathways for the biosynthesis of industrial chemicals: 3-hydroxypropanoate. Biotechnol. Bioeng. 106, 462-473 PubMed.
    • (2010) Biotechnol. Bioeng , vol.106 , pp. 462-473
    • Henry, C.S.1    Broadbelt, L.J.2    Hatzimanikatis, V.3
  • 23
    • 77956696072 scopus 로고    scopus 로고
    • High-throughput generation, optimization, and analysis of genome-scale metabolic models
    • CrossRef PubMed
    • Henry, C.S., DeJongh, M., Best, A.A., Frybarger, P.M., Linsay, B. and Stevens, R.L. (2010) High-throughput generation, optimization, and analysis of genome-scale metabolic models. Nat. Biotechnol. 28, 977-982 CrossRef PubMed.
    • (2010) Nat. Biotechnol , vol.28 , pp. 977-982
    • Henry, C.S.1    DeJongh, M.2    Best, A.A.3    Frybarger, P.M.4    Linsay, B.5    Stevens, R.L.6
  • 26
    • 84871588520 scopus 로고    scopus 로고
    • Systems-level characterization of a host-microbe metabolic symbiosis in the mammalian gut
    • CrossRef PubMed
    • Heinken, A., Sahoo, S., Fleming, R.M. and Thiele, I. (2013) Systems-level characterization of a host-microbe metabolic symbiosis in the mammalian gut. Gut Microbes 4, 28-40 CrossRef PubMed.
    • (2013) Gut Microbes , vol.4 , pp. 28-40
    • Heinken, A.1    Sahoo, S.2    Fleming, R.M.3    Thiele, I.4
  • 27
    • 67650573077 scopus 로고    scopus 로고
    • IBsu1103: A new genome-scale metabolic model of Bacillus subtilis based on SEED annotations
    • CrossRef PubMed
    • Henry, C.S., Zinner, J.F., Cohoon, M.P. and Stevens, R.L. (2009) iBsu1103: a new genome-scale metabolic model of Bacillus subtilis based on SEED annotations. Genome Biol. 10, R69 CrossRef PubMed.
    • (2009) Genome Biol , vol.10 , pp. R69
    • Henry, C.S.1    Zinner, J.F.2    Cohoon, M.P.3    Stevens, R.L.4
  • 28
    • 79960558167 scopus 로고    scopus 로고
    • IRsp1095: A genome-scale reconstruction of the Rhodobacter sphaeroides metabolic network
    • CrossRef PubMed
    • Imam, S., Yilmaz, S., Sohmen, U., Gorzalski, A.S., Reed, J. L., Noguera, D.R. and Donohue, T. J. (2011) iRsp1095: a genome-scale reconstruction of the Rhodobacter sphaeroides metabolic network. BMC Syst. Biol. 5, 116 CrossRef PubMed.
    • (2011) BMC Syst. Biol , vol.5 , pp. 116
    • Imam, S.1    Yilmaz, S.2    Sohmen, U.3    Gorzalski, A.S.4    Reed, J.L.5    Noguera, D.R.6    Donohue, T.J.7
  • 29
    • 79952789318 scopus 로고    scopus 로고
    • An experimentally validated genome-scale metabolic reconstruction of Klebsiella pneumoniae MGH 78578, iYL1228
    • CrossRef PubMed
    • Liao, Y.C., Huang, T.W., Chen, F.C., Charusanti, P., Hong, J.S., Chang, H.Y., Tsai, S.F., Palsson, B.O. and Hsiung, C.A. (2011) An experimentally validated genome-scale metabolic reconstruction of Klebsiella pneumoniae MGH 78578, iYL1228. J. Bacteriol. 193, 1710-1717 CrossRef PubMed.
    • (2011) J. Bacteriol. , vol.193 , pp. 1710-1717
    • Liao, Y.C.1    Huang, T.W.2    Chen, F.C.3    Charusanti, P.4    Hong, J.S.5    Chang, H.Y.6    Tsai, S.F.7    Palsson, B.O.8    Hsiung, C.A.9
  • 30
    • 84857137366 scopus 로고    scopus 로고
    • Detailing the optimality of photosynthesis in cyanobacteria through systems biology analysis
    • CrossRef PubMed
    • Nogales, J., Gudmundsson, S., Knight, E.M., Palsson, B.O. and Thiele, I. (2012) Detailing the optimality of photosynthesis in cyanobacteria through systems biology analysis. Proc. Natl. Acad. Sci. U.S.A. 109, 2678-2683 CrossRef PubMed.
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 2678-2683
    • Nogales, J.1    Gudmundsson, S.2    Knight, E.M.3    Palsson, B.O.4    Thiele, I.5
  • 31
    • 80054069179 scopus 로고    scopus 로고
    • A comprehensive genome-scale reconstruction of Escherichia coli metabolism-2011
    • CrossRef PubMed
    • Orth, J.D., Conrad, T.M., Na, J., Lerman, J.A., Nam, H., Feist, A.M. and Palsson, B.O. (2011) A comprehensive genome-scale reconstruction of Escherichia coli metabolism-2011. Mol. Syst. Biol. 7, 535 CrossRef PubMed.
    • (2011) Mol. Syst. Biol , vol.7 , pp. 535
    • Orth, J.D.1    Conrad, T.M.2    Na, J.3    Lerman, J.A.4    Nam, H.5    Feist, A.M.6    Palsson, B.O.7
  • 32
    • 65649126379 scopus 로고    scopus 로고
    • Connecting extracellular metabolomic measurements to intracellular flux states in yeast
    • CrossRef PubMed
    • Mo, M.L., Palsson, B.O. and Herrgard, M.J. (2009) Connecting extracellular metabolomic measurements to intracellular flux states in yeast. BMC Syst. Biol. 3, 37 CrossRef PubMed.
    • (2009) BMC Syst. Biol. , vol.3 , pp. 37
    • Mo, M.L.1    Palsson, B.O.2    Herrgard, M.J.3
  • 33
    • 84928045239 scopus 로고    scopus 로고
    • Improved evidence-based genome-scale metabolic models for maize leaf, embryo, and endosperm
    • CrossRef PubMed
    • Seaver, S.M., Bradbury, L.M., Frelin, O., Zarecki, R., Ruppin, E., Hanson, A.D. and Henry, C.S. (2015) Improved evidence-based genome-scale metabolic models for maize leaf, embryo, and endosperm. Front. Plant Sci. 6, 142 CrossRef PubMed.
    • (2015) Front. Plant Sci. , vol.6 , pp. 142
    • Seaver, S.M.1    Bradbury, L.M.2    Frelin, O.3    Zarecki, R.4    Ruppin, E.5    Hanson, A.D.6    Henry, C.S.7
  • 34
    • 57649123534 scopus 로고    scopus 로고
    • Global phenotypic characterization of bacteria
    • CrossRef PubMed
    • Bochner, B.R. (2009) Global phenotypic characterization of bacteria. FEMS Microbiol. Rev. 33, 191-205 CrossRef PubMed.
    • (2009) FEMS Microbiol. Rev , vol.33 , pp. 191-205
    • Bochner, B.R.1
  • 35
    • 1642457253 scopus 로고    scopus 로고
    • The effects of alternate optimal solutions in constraint-based genome-scale metabolic models
    • CrossRef PubMed
    • Mahadevan, R. and Schilling, C.H. (2003) The effects of alternate optimal solutions in constraint-based genome-scale metabolic models. Metab. Eng. 5, 264-276 CrossRef PubMed.
    • (2003) Metab. Eng , vol.5 , pp. 264-276
    • Mahadevan, R.1    Schilling, C.H.2
  • 36
    • 45749137952 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase involved in riboflavin biosynthesis
    • CrossRef PubMed
    • Magalhaes, M.L., Argyrou, A., Cahill, S.M. and Blanchard, J.S. (2008) Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase involved in riboflavin biosynthesis. Biochemistry 47, 6499-6507 CrossRef PubMed.
    • (2008) Biochemistry , vol.47 , pp. 6499-6507
    • Magalhaes, M.L.1    Argyrou, A.2    Cahill, S.M.3    Blanchard, J.S.4
  • 38
    • 77957909920 scopus 로고    scopus 로고
    • The photosensitive phs1 mutant is impaired in the riboflavin biogenesis pathway
    • CrossRef PubMed
    • Ouyang, M., Ma, J., Zou, M., Guo, J., Wang, L., Lu, C. and Zhang, L. (2010) The photosensitive phs1 mutant is impaired in the riboflavin biogenesis pathway. J. Plant Physiol. 167, 1466-1476 CrossRef PubMed.
    • (2010) J. Plant Physiol , vol.167 , pp. 1466-1476
    • Ouyang, M.1    Ma, J.2    Zou, M.3    Guo, J.4    Wang, L.5    Lu, C.6    Zhang, L.7
  • 40
    • 0017072736 scopus 로고
    • Transition state analogs for thiamin pyrophosphate-dependent enzymes
    • PubMed
    • Gutowski, J.A. and Lienhard, G.E. (1976) Transition state analogs for thiamin pyrophosphate-dependent enzymes. J. Biol. Chem. 251, 2863-2866 PubMed.
    • (1976) J. Biol. Chem , vol.251 , pp. 2863-2866
    • Gutowski, J.A.1    Lienhard, G.E.2
  • 41
    • 70349629097 scopus 로고
    • Mechanism of action of transketolase. I. Properties of the crystalline yeast enzyme
    • Datta, A.G. and Racker, E. (1961) Mechanism of action of transketolase. I. Properties of the crystalline yeast enzyme. J. Biol. Chem. 236, 617-623.
    • (1961) J. Biol. Chem , vol.236 , pp. 617-623
    • Datta, A.G.1    Racker, E.2
  • 42
    • 84883313454 scopus 로고    scopus 로고
    • A cross-kingdom Nudix enzyme that pre-empts damage in thiamin metabolism
    • CrossRef PubMed
    • Goyer, A., Hasnain, G., Frelin, O., Ralat, M.A., Gregory 3rd, J.F. and Hanson, A.D. (2013) A cross-kingdom Nudix enzyme that pre-empts damage in thiamin metabolism. Biochem. J. 454, 533-542 CrossRef PubMed.
    • (2013) Biochem. J , vol.454 , pp. 533-542
    • Goyer, A.1    Hasnain, G.2    Frelin, O.3    Ralat, M.A.4    Gregory, J.F.5    Hanson, A.D.6
  • 43
    • 0029000244 scopus 로고
    • Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus
    • CrossRef
    • Legrain, C., Demarez, M., Glansdorff, N. and Pierard, A. (1995) Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus. Microbiology 141, 1093-1099 CrossRef.
    • (1995) Microbiology , vol.141 , pp. 1093-1099
    • Legrain, C.1    Demarez, M.2    Glansdorff, N.3    Pierard, A.4
  • 44
    • 84961985801 scopus 로고    scopus 로고
    • Mechanism of thermal decomposition of carbamoyl phosphate and its stabilization by aspartate and ornithine transcarbamoylases
    • CrossRef PubMed
    • Wang, Q., Xia, J., Guallar, V., Krilov, G. and Kantrowitz, E.R. (2008) Mechanism of thermal decomposition of carbamoyl phosphate and its stabilization by aspartate and ornithine transcarbamoylases. Proc. Natl. Acad. Sci. U.S.A. 105, 16918-16923 CrossRef PubMed.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 16918-16923
    • Wang, Q.1    Xia, J.2    Guallar, V.3    Krilov, G.4    Kantrowitz, E.R.5
  • 45
    • 0033525887 scopus 로고    scopus 로고
    • Channeling of carbamoyl phosphate to the pyrimidine and arginine biosynthetic pathways in the deep sea hyperthermophilic archaeon Pyrococcus abyssi
    • CrossRef PubMed
    • Purcarea, C., Evans, D.R. and Herve, G. (1999) Channeling of carbamoyl phosphate to the pyrimidine and arginine biosynthetic pathways in the deep sea hyperthermophilic archaeon Pyrococcus abyssi. J. Biol. Chem. 274, 6122-6129 CrossRef PubMed.
    • (1999) J. Biol. Chem , vol.274 , pp. 6122-6129
    • Purcarea, C.1    Evans, D.R.2    Herve, G.3
  • 46
    • 84874621176 scopus 로고    scopus 로고
    • RidA proteins prevent metabolic damage inflicted by PLP-dependent dehydratases in all domains of life
    • CrossRef PubMed
    • Lambrecht, J.A., Schmitz, G.E. and Downs, D.M. (2013) RidA proteins prevent metabolic damage inflicted by PLP-dependent dehydratases in all domains of life. MBio 4, e00033-e00013 CrossRef PubMed.
    • (2013) MBio , vol.4 , pp. e00033-e000113
    • Lambrecht, J.A.1    Schmitz, G.E.2    Downs, D.M.3
  • 49
    • 84866123900 scopus 로고    scopus 로고
    • An accelerated workflow for untargeted metabolomics using the METLIN database
    • CrossRef PubMed
    • Tautenhahn, R., Cho, K., Uritboonthai, W., Zhu, Z., Patti, G.J. and Siuzdak, G. (2012) An accelerated workflow for untargeted metabolomics using the METLIN database. Nat. Biotechnol. 30, 826-828 CrossRef PubMed.
    • (2012) Nat. Biotechnol , vol.30 , pp. 826-828
    • Tautenhahn, R.1    Cho, K.2    Uritboonthai, W.3    Zhu, Z.4    Patti, G.J.5    Siuzdak, G.6
  • 50
    • 0022973968 scopus 로고
    • Substrate specificity of bovine liver formaldehyde dehydrogenase
    • PubMed
    • Pourmotabbed, T. and Creighton, D.J. (1986) Substrate specificity of bovine liver formaldehyde dehydrogenase. J. Biol. Chem. 261, 14240-14244 PubMed.
    • (1986) J. Biol. Chem , vol.261 , pp. 14240-14244
    • Pourmotabbed, T.1    Creighton, D.J.2
  • 51
    • 0028850950 scopus 로고
    • Α-Ketoacids scavenge H2O2 in vitro and in vivo and reduce menadione-induced DNA injury and cytotoxicity
    • PubMed
    • Nath, K.A., Ngo, E.O., Hebbel, R.P., Croatt, A.J., Zhou, B. and Nutter, L.M. (1995) α-Ketoacids scavenge H2O2 in vitro and in vivo and reduce menadione-induced DNA injury and cytotoxicity. Am. J. Physiol. 268, C227-C336 PubMed.
    • (1995) Am. J. Physiol , vol.268 , pp. C227-C336
    • Nath, K.A.1    Ngo, E.O.2    Hebbel, R.P.3    Croatt, A.J.4    Zhou, B.5    Nutter, L.M.6
  • 52
    • 80054925355 scopus 로고    scopus 로고
    • Eating for two: How metabolism establishes interspecies interactions in the gut
    • CrossRef PubMed
    • Fischbach, M.A. and Sonnenburg, J.L. (2011) Eating for two: how metabolism establishes interspecies interactions in the gut. Cell Host Microbe 10, 336-347 CrossRef PubMed.
    • (2011) Cell Host Microbe , vol.10 , pp. 336-347
    • Fischbach, M.A.1    Sonnenburg, J.L.2
  • 53
    • 0016736757 scopus 로고
    • The energy-coupling controlled efflux of 2-keto-3-deoxy-d-gluconate in Escherichia coli K12
    • CrossRef PubMed
    • Lagarde, A.E. and Stoeber, F.R. (1975) The energy-coupling controlled efflux of 2-keto-3-deoxy-d-gluconate in Escherichia coli K12. Eur. J. Biochem. 55, 343-354 CrossRef PubMed.
    • (1975) Eur. J. Biochem , vol.55 , pp. 343-354
    • Lagarde, A.E.1    Stoeber, F.R.2
  • 55
    • 0025611278 scopus 로고
    • The enzymes of detoxication
    • PubMed
    • Jakoby, W.B. and Ziegler, D.M. (1990) The enzymes of detoxication. J. Biol. Chem. 265, 20715-20178 PubMed.
    • (1990) J. Biol. Chem , vol.265 , pp. 20178-20715
    • Jakoby, W.B.1    Ziegler, D.M.2
  • 56
    • 77955042462 scopus 로고    scopus 로고
    • From complete genome sequence to 'complete' understanding?
    • CrossRef PubMed
    • Galperin, M.Y. and Koonin, E.V. (2010) From complete genome sequence to 'complete' understanding? Trends Biotechnol. 28, 398-406 CrossRef PubMed.
    • (2010) Trends Biotechnol , vol.28 , pp. 398-406
    • Galperin, M.Y.1    Koonin, E.V.2
  • 57
    • 0347419281 scopus 로고    scopus 로고
    • Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation
    • CrossRef PubMed
    • Thornalley, P.J. (2003) Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation. Biochem. Soc. Trans. 31, 1343-1348 CrossRef PubMed.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 1343-1348
    • Thornalley, P.J.1
  • 60
    • 0343007769 scopus 로고
    • The enzymic hydrolysis of glutamine and its spontaneous decomposition in buffer solutions
    • CrossRef
    • Bray, H.G., James, S.P., Raffan, I.R. and Thorpe, W.V. (1949) The enzymic hydrolysis of glutamine and its spontaneous decomposition in buffer solutions. Biochem. J. 44, 625-627 CrossRef.
    • (1949) Biochem. J. , vol.44 , pp. 625-627
    • Bray, H.G.1    James, S.P.2    Raffan, I.R.3    Thorpe, W.V.4
  • 61
    • 0021471746 scopus 로고
    • Acid-base catalysis of the elimination and isomerization reactions of triose phosphates
    • CrossRef
    • Richard, J.P. (1984) Acid-base catalysis of the elimination and isomerization reactions of triose phosphates. J. Am. Chem. Soc. 106, 4926-4936 CrossRef.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 4926-4936
    • Richard, J.P.1


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