메뉴 건너뛰기




Volumn 44, Issue , 2017, Pages 150-159

Metabolite damage and repair in metabolic engineering design

Author keywords

Enzyme promiscuity; Metabolic engineering; Metabolite damage; Metabolite repair; Side reaction; Synthetic biology

Indexed keywords

BIOCHEMICAL ENGINEERING; BIOMOLECULES; DAMAGE DETECTION; ENZYMES; METABOLISM; METABOLITES; PRODUCT DESIGN; REPAIR;

EID: 85031774799     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2017.10.006     Document Type: Review
Times cited : (39)

References (100)
  • 1
    • 0024293228 scopus 로고
    • Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration
    • Acheson, S.A., Kirkman, H.N., Wolfenden, R., Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration. Biochemistry 27:19 (1988), 7371–7375, 10.1021/bi00419a030.
    • (1988) Biochemistry , vol.27 , Issue.19 , pp. 7371-7375
    • Acheson, S.A.1    Kirkman, H.N.2    Wolfenden, R.3
  • 2
    • 85031775660 scopus 로고    scopus 로고
    • New Microorganism and Method for the Production of 1,2-propanediol based on NADPH Dependent Acetol Reductase and Improved NADPH supply. United States Patent Application Publication No. US2017 0145446 A1.
    • Aliprandi, P., Navarro, E., Raynaud, C., Bestel Corre, G., Soucaille, P., 2017. New Microorganism and Method for the Production of 1,2-propanediol based on NADPH Dependent Acetol Reductase and Improved NADPH supply. United States Patent Application Publication No. US2017 0145446 A1.
    • (2017)
    • Aliprandi, P.1    Navarro, E.2    Raynaud, C.3    Bestel Corre, G.4    Soucaille, P.5
  • 3
    • 85009154900 scopus 로고    scopus 로고
    • Deep metabolome annotation in natural products research: towards a virtuous cycle in metabolite identification
    • Allard, P.-M., Genta-Jouve, G., Wolfender, J.-L., Deep metabolome annotation in natural products research: towards a virtuous cycle in metabolite identification. Curr. Opin. Chem. Biol. 36 (2017), 40–49, 10.1016/j.cbpa.2016.12.022.
    • (2017) Curr. Opin. Chem. Biol. , vol.36 , pp. 40-49
    • Allard, P.-M.1    Genta-Jouve, G.2    Wolfender, J.-L.3
  • 4
    • 0034727672 scopus 로고    scopus 로고
    • Hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate at pH 2.5 to 4.5
    • Baggott, J.E., Hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate at pH 2.5 to 4.5. Biochemistry 39:47 (2000), 14647–14653, 10.1021/bi001362m.
    • (2000) Biochemistry , vol.39 , Issue.47 , pp. 14647-14653
    • Baggott, J.E.1
  • 5
    • 84994772022 scopus 로고    scopus 로고
    • A guardian angel phosphatase for mainline carbon metabolism
    • Beaudoin, G.A., Hanson, A.D., A guardian angel phosphatase for mainline carbon metabolism. Trends Biochem. Sci. 41 (2016), 893–894, 10.1016/j.tibs.2016.08.005.
    • (2016) Trends Biochem. Sci. , vol.41 , pp. 893-894
    • Beaudoin, G.A.1    Hanson, A.D.2
  • 6
    • 84890057926 scopus 로고    scopus 로고
    • The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life
    • Beld, J., Sonnenschein, E.C., Vickery, C.R., Noel, J.P., Burkart, M.D., The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life. Nat. Prod. Rep. 31:1 (2014), 61–108, 10.1039/c3np70054b.
    • (2014) Nat. Prod. Rep. , vol.31 , Issue.1 , pp. 61-108
    • Beld, J.1    Sonnenschein, E.C.2    Vickery, C.R.3    Noel, J.P.4    Burkart, M.D.5
  • 7
    • 77953580280 scopus 로고    scopus 로고
    • Exploiting cell-free systems: implementation and debugging of a system of biotransformations
    • Bujara, M., Schümperli, M., Billerbeck, S., Heinemann, M., Panke, S., Exploiting cell-free systems: implementation and debugging of a system of biotransformations. Biotechnol. Bioeng. 106:3 (2010), 376–389, 10.1002/bit.22666.
    • (2010) Biotechnol. Bioeng. , vol.106 , Issue.3 , pp. 376-389
    • Bujara, M.1    Schümperli, M.2    Billerbeck, S.3    Heinemann, M.4    Panke, S.5
  • 8
    • 84964509986 scopus 로고    scopus 로고
    • Development of a commercial scale process for production of 1,4-butanediol from sugar
    • Burgard, A., Burk, M.J., Osterhout, R., Van Dien, S., Yim, H., Development of a commercial scale process for production of 1,4-butanediol from sugar. Curr. Opin. Biotechnol. 42 (2016), 118–125, 10.1016/j.copbio.2016.04.016.
    • (2016) Curr. Opin. Biotechnol. , vol.42 , pp. 118-125
    • Burgard, A.1    Burk, M.J.2    Osterhout, R.3    Van Dien, S.4    Yim, H.5
  • 9
    • 0033532073 scopus 로고    scopus 로고
    • A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli
    • Cai, H., Clarke, S., A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli. J. Biol. Chem. 274:19 (1999), 13470–13479, 10.1074/jbc.274.19.13470.
    • (1999) J. Biol. Chem. , vol.274 , Issue.19 , pp. 13470-13479
    • Cai, H.1    Clarke, S.2
  • 11
    • 77954886383 scopus 로고    scopus 로고
    • Biocatalytic properties of a recombinant Fusarium proliferatum lactonase with significantly enhanced production by optimal expression in Escherichia coli
    • Chen, B., Fan, L.Q., Xu, J.H., Zhao, J., Zhang, X., Ouyang, L.M., Biocatalytic properties of a recombinant Fusarium proliferatum lactonase with significantly enhanced production by optimal expression in Escherichia coli. Appl. Biochem. Biotechnol. 162:3 (2010), 744–756, 10.1007/s12010-009-8819-1.
    • (2010) Appl. Biochem. Biotechnol. , vol.162 , Issue.3 , pp. 744-756
    • Chen, B.1    Fan, L.Q.2    Xu, J.H.3    Zhao, J.4    Zhang, X.5    Ouyang, L.M.6
  • 12
    • 84868628420 scopus 로고    scopus 로고
    • Synthetic pathway for production of five-carbon alcohols from isopentenyl diphosphate
    • Chou, H.H., Keasling, J.D., Synthetic pathway for production of five-carbon alcohols from isopentenyl diphosphate. Appl. Environ. Microbiol. 78:22 (2012), 7849–7855, 10.1128/AEM.01175-12.
    • (2012) Appl. Environ. Microbiol. , vol.78 , Issue.22 , pp. 7849-7855
    • Chou, H.H.1    Keasling, J.D.2
  • 14
    • 84901378109 scopus 로고    scopus 로고
    • Screening of metagenomic and genomic libraries reveals three classes of bacterial enzymes that overcome the toxicity of acrylate
    • Curson, A.R., Burns, O.J., Voget, S., Daniel, R., Todd, J.D., McInnis, K., Wexler, M., Johnston, A.W., Screening of metagenomic and genomic libraries reveals three classes of bacterial enzymes that overcome the toxicity of acrylate. PLoS One, 9(5), 2014, e97660, 10.1371/journal.pone.0097660.
    • (2014) PLoS One , vol.9 , Issue.5 , pp. e97660
    • Curson, A.R.1    Burns, O.J.2    Voget, S.3    Daniel, R.4    Todd, J.D.5    McInnis, K.6    Wexler, M.7    Johnston, A.W.8
  • 15
    • 85007505790 scopus 로고    scopus 로고
    • Coping with inevitable accidents in metabolism
    • Danchin, A., Coping with inevitable accidents in metabolism. Microb. Biotechnol. 10:1 (2017), 57–72, 10.1111/1751-7915.12461.
    • (2017) Microb. Biotechnol. , vol.10 , Issue.1 , pp. 57-72
    • Danchin, A.1
  • 16
    • 0033820420 scopus 로고    scopus 로고
    • Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase
    • Delpierre, G., Rider, M.H., Collard, F., Stroobant, V., Vanstapel, F., Santos, H., Van Schaftingen, E., Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes 49:10 (2000), 1627–1634, 10.2337/diabetes.49.10.1627.
    • (2000) Diabetes , vol.49 , Issue.10 , pp. 1627-1634
    • Delpierre, G.1    Rider, M.H.2    Collard, F.3    Stroobant, V.4    Vanstapel, F.5    Santos, H.6    Van Schaftingen, E.7
  • 17
    • 33846229270 scopus 로고    scopus 로고
    • Non-enzymatic interactions of glyoxylate with lysine, arginine, and glucosamine: a study of advanced non-enzymatic glycation like compounds
    • Dutta, U., Cohenford, M.A., Guha, M., Dain, J.A., Non-enzymatic interactions of glyoxylate with lysine, arginine, and glucosamine: a study of advanced non-enzymatic glycation like compounds. Bioorg. Chem. 35:1 (2007), 11–24, 10.1016/j.bioorg.2006.07.005.
    • (2007) Bioorg. Chem. , vol.35 , Issue.1 , pp. 11-24
    • Dutta, U.1    Cohenford, M.A.2    Guha, M.3    Dain, J.A.4
  • 18
    • 85028355868 scopus 로고    scopus 로고
    • Bioremediation 3.0: engineering pollutant-removing bacteria in the times of systemic biology
    • Dvořák, P., Nikel, P.I., Damborský, J., de Lorenzo, V., Bioremediation 3.0: engineering pollutant-removing bacteria in the times of systemic biology. Biotechnol. Adv. 35:7 (2017), 845–866, 10.1016/j.biotechadv.2017.08.001.
    • (2017) Biotechnol. Adv. , vol.35 , Issue.7 , pp. 845-866
    • Dvořák, P.1    Nikel, P.I.2    Damborský, J.3    de Lorenzo, V.4
  • 19
    • 77749279783 scopus 로고    scopus 로고
    • The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/ß-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase
    • Erb, T.J., Frerichs-Revermann, L., Fuchs, G., Alber, B.E., The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/ß-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase. J. Bacteriol. 192:5 (2010), 1249–1258, 10.1128/JB.01267-09.
    • (2010) J. Bacteriol. , vol.192 , Issue.5 , pp. 1249-1258
    • Erb, T.J.1    Frerichs-Revermann, L.2    Fuchs, G.3    Alber, B.E.4
  • 20
    • 85010908796 scopus 로고    scopus 로고
    • Synthetic metabolism: metabolic engineering meets enzyme design
    • Erb, T.J., Jones, P.R., Bar-Even, A., Synthetic metabolism: metabolic engineering meets enzyme design. Curr. Opin. Chem. Biol. 37 (2017), 56–62, 10.1016/j.cbpa.2016.12.023.
    • (2017) Curr. Opin. Chem. Biol. , vol.37 , pp. 56-62
    • Erb, T.J.1    Jones, P.R.2    Bar-Even, A.3
  • 23
    • 79959898098 scopus 로고    scopus 로고
    • Extending biochemical databases by metabolomic surveys
    • Fiehn, O., Barupal, D.K., Kind, T., Extending biochemical databases by metabolomic surveys. J. Biol. Chem. 286:27 (2011), 23637–23643, 10.1074/jbc.R110.173617.
    • (2011) J. Biol. Chem. , vol.286 , Issue.27 , pp. 23637-23643
    • Fiehn, O.1    Barupal, D.K.2    Kind, T.3
  • 24
    • 21744454994 scopus 로고    scopus 로고
    • Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme
    • Fortpied, J., Gemayel, R., Stroobant, V., van Schaftingen, E., Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme. Biochem. J. 388:3 (2005), 795–802, 10.1042/BJ20041976.
    • (2005) Biochem. J. , vol.388 , Issue.3 , pp. 795-802
    • Fortpied, J.1    Gemayel, R.2    Stroobant, V.3    van Schaftingen, E.4
  • 25
    • 34548128354 scopus 로고    scopus 로고
    • Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation
    • Gemayel, R., Fortpied, J., Rzem, R., Vertommen, D., Veiga-da-Cunha, M., Van Schaftingen, E., Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation. FEBS J. 274:17 (2007), 4360–4374, 10.1111/j.1742-4658.2007.05948.x.
    • (2007) FEBS J. , vol.274 , Issue.17 , pp. 4360-4374
    • Gemayel, R.1    Fortpied, J.2    Rzem, R.3    Vertommen, D.4    Veiga-da-Cunha, M.5    Van Schaftingen, E.6
  • 26
    • 0030277436 scopus 로고    scopus 로고
    • The other side of metabolism: a review
    • Golubev, A.G., The other side of metabolism: a review. Biochemistry 61:11 (1996), 2018–2039.
    • (1996) Biochemistry , vol.61 , Issue.11 , pp. 2018-2039
    • Golubev, A.G.1
  • 27
    • 84968813917 scopus 로고    scopus 로고
    • Metabolite damage and metabolite damage control in plants
    • Hanson, A.D., Henry, C.S., Fiehn, O., de Crécy-Lagard, V., Metabolite damage and metabolite damage control in plants. Annu. Rev. Plant Biol. 67 (2016), 131–152, 10.1146/annurev-arplant-043015-111648.
    • (2016) Annu. Rev. Plant Biol. , vol.67 , pp. 131-152
    • Hanson, A.D.1    Henry, C.S.2    Fiehn, O.3    de Crécy-Lagard, V.4
  • 28
    • 72449145463 scopus 로고    scopus 로고
    • 'Unknown' proteins and ‘orphan’ enzymes: the missing half of the engineering parts list – and how to find it
    • Hanson, A.D., Pribat, A., Waller, J.C., de Crécy-Lagard, V., ‘Unknown’ proteins and ‘orphan’ enzymes: the missing half of the engineering parts list – and how to find it. Biochem. J. 425:1 (2009), 1–11, 10.1042/BJ20091328.
    • (2009) Biochem. J. , vol.425 , Issue.1 , pp. 1-11
    • Hanson, A.D.1    Pribat, A.2    Waller, J.C.3    de Crécy-Lagard, V.4
  • 30
    • 0035068571 scopus 로고    scopus 로고
    • Role of type II thioesterases: evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units
    • Heathcote, M.L., Staunton, J., Leadlay, P.F., Role of type II thioesterases: evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units. Chem. Biol. 8:2 (2001), 207–220, 10.1016/S1074-5521(01)00002-3.
    • (2001) Chem. Biol. , vol.8 , Issue.2 , pp. 207-220
    • Heathcote, M.L.1    Staunton, J.2    Leadlay, P.F.3
  • 31
    • 84957104073 scopus 로고    scopus 로고
    • Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?
    • Horsman, M.E., Hari, T.P., Boddy, C.N., Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?. Nat. Prod. Rep. 33:2 (2016), 183–202, 10.1039/c4np00148f.
    • (2016) Nat. Prod. Rep. , vol.33 , Issue.2 , pp. 183-202
    • Horsman, M.E.1    Hari, T.P.2    Boddy, C.N.3
  • 33
    • 84999016796 scopus 로고    scopus 로고
    • Ophthalmic acid accumulation in an Escherichia coli mutant lacking the conserved pyridoxal 5'-phosphate-binding protein YggS
    • Ito, T., Yamauchi, A., Hemmi, H., Yoshimura, T., Ophthalmic acid accumulation in an Escherichia coli mutant lacking the conserved pyridoxal 5'-phosphate-binding protein YggS. J. Biosci. Bioeng. 122:6 (2016), 689–693, 10.1016/j.jbiosc.2016.06.010.
    • (2016) J. Biosci. Bioeng. , vol.122 , Issue.6 , pp. 689-693
    • Ito, T.1    Yamauchi, A.2    Hemmi, H.3    Yoshimura, T.4
  • 36
    • 84891760956 scopus 로고    scopus 로고
    • Data, information, knowledge and principle: back to metabolism in KEGG
    • Kanehisa, M., Goto, S., Sato, Y., Kawashima, M., Furumichi, M., Tanabe, M., Data, information, knowledge and principle: back to metabolism in KEGG. Nucleic Acids Res. 42 (2014), D199–D205, 10.1093/nar/gkt1076.
    • (2014) Nucleic Acids Res. , vol.42 , pp. D199-D205
    • Kanehisa, M.1    Goto, S.2    Sato, Y.3    Kawashima, M.4    Furumichi, M.5    Tanabe, M.6
  • 37
    • 84921468648 scopus 로고    scopus 로고
    • The widespread role of non-enzymatic reactions in cellular metabolism
    • Keller, M.A., Piedrafita, G., Ralser, M., The widespread role of non-enzymatic reactions in cellular metabolism. Curr. Opin. Biotechnol. 34 (2015), 153–161, 10.1016/j.copbio.2014.12.020.
    • (2015) Curr. Opin. Biotechnol. , vol.34 , pp. 153-161
    • Keller, M.A.1    Piedrafita, G.2    Ralser, M.3
  • 39
    • 84906951494 scopus 로고    scopus 로고
    • Roles of type II thioesterases and their application for secondary metabolite yield improvement
    • Kotowska, M., Pawlik, K., Roles of type II thioesterases and their application for secondary metabolite yield improvement. Appl. Microbiol. Biotechnol. 98:18 (2014), 7735–7746, 10.1007/s00253-014-5952-8.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , Issue.18 , pp. 7735-7746
    • Kotowska, M.1    Pawlik, K.2
  • 40
    • 67449126832 scopus 로고    scopus 로고
    • Assay and purification of omega-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the α-keto acid analogues of glutamine and asparagine
    • Krasnikov, B.F., Nostramo, R., Pinto, J.T., Cooper, A.J., Assay and purification of omega-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the α-keto acid analogues of glutamine and asparagine. Anal. Biochem. 391:2 (2009), 144–150, 10.1016/j.ab.2009.05.025.
    • (2009) Anal. Biochem. , vol.391 , Issue.2 , pp. 144-150
    • Krasnikov, B.F.1    Nostramo, R.2    Pinto, J.T.3    Cooper, A.J.4
  • 41
    • 84864826447 scopus 로고    scopus 로고
    • Pyroglutamic acid: throwing light on a lightly studied metabolite
    • Kumar, A., Bachhawat, A.K., Pyroglutamic acid: throwing light on a lightly studied metabolite. Curr. Sci. 102:2 (2012), 288–297 〈http://www.jstor.org/stable/24083854〉.
    • (2012) Curr. Sci. , vol.102 , Issue.2 , pp. 288-297
    • Kumar, A.1    Bachhawat, A.K.2
  • 42
    • 78651227092 scopus 로고    scopus 로고
    • The biological significance of methionine sulfoxide stereochemistry
    • Lee, B.C., Gladyshev, V.N., The biological significance of methionine sulfoxide stereochemistry. Free Radic. Biol. Med. 50:2 (2011), 221–227, 10.1016/j.freeradbiomed.2010.11.008.
    • (2011) Free Radic. Biol. Med. , vol.50 , Issue.2 , pp. 221-227
    • Lee, B.C.1    Gladyshev, V.N.2
  • 45
    • 84872715396 scopus 로고    scopus 로고
    • Metabolite damage and its repair or pre-emption
    • Linster, C.L., Van Schaftingen, E., Hanson, A.D., Metabolite damage and its repair or pre-emption. Nat. Chem. Biol. 9:2 (2013), 72–80, 10.1038/nchembio.1141.
    • (2013) Nat. Chem. Biol. , vol.9 , Issue.2 , pp. 72-80
    • Linster, C.L.1    Van Schaftingen, E.2    Hanson, A.D.3
  • 46
    • 84893447906 scopus 로고    scopus 로고
    • From the selfish gene to selfish metabolism: revisiting the central dogma
    • de Lorenzo, V., From the selfish gene to selfish metabolism: revisiting the central dogma. Bioessays 36:3 (2014), 226–235, 10.1002/bies.201300153.
    • (2014) Bioessays , vol.36 , Issue.3 , pp. 226-235
    • de Lorenzo, V.1
  • 47
    • 84934300609 scopus 로고    scopus 로고
    • Chemical reactivity drives spatiotemporal organisation of bacterial metabolism
    • de Lorenzo, V., Sekowska, A., Danchin, A., Chemical reactivity drives spatiotemporal organisation of bacterial metabolism. FEMS Microbiol. Rev. 39:1 (2015), 96–119, 10.1111/1574-6976.12089.
    • (2015) FEMS Microbiol. Rev. , vol.39 , Issue.1 , pp. 96-119
    • de Lorenzo, V.1    Sekowska, A.2    Danchin, A.3
  • 48
    • 1642457253 scopus 로고    scopus 로고
    • The effects of alternate optimal solutions in constraint-based genome-scale metabolic models
    • Mahadevan, R., Schilling, C.H., The effects of alternate optimal solutions in constraint-based genome-scale metabolic models. Metab. Eng. 5:4 (2003), 264–276, 10.1016/j.ymben.2003.09.002.
    • (2003) Metab. Eng. , vol.5 , Issue.4 , pp. 264-276
    • Mahadevan, R.1    Schilling, C.H.2
  • 49
    • 82355171918 scopus 로고    scopus 로고
    • Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair
    • Marbaix, A.Y., Noël, G., Detroux, A.M., Vertommen, D., Van Schaftingen, E., Linster, C.L., Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair. J. Biol. Chem. 286:48 (2011), 41246–41252, 10.1074/jbc.C111.310847.
    • (2011) J. Biol. Chem. , vol.286 , Issue.48 , pp. 41246-41252
    • Marbaix, A.Y.1    Noël, G.2    Detroux, A.M.3    Vertommen, D.4    Van Schaftingen, E.5    Linster, C.L.6
  • 50
    • 0038391517 scopus 로고    scopus 로고
    • Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
    • Martin, V.J., Pitera, D.J., Withers, S.T., Newman, J.D., Keasling, J.D., Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nat. Biotechnol. 21:7 (2003), 796–802, 10.1038/nbt833.
    • (2003) Nat. Biotechnol. , vol.21 , Issue.7 , pp. 796-802
    • Martin, V.J.1    Pitera, D.J.2    Withers, S.T.3    Newman, J.D.4    Keasling, J.D.5
  • 54
    • 0001010357 scopus 로고
    • Control of aspartate beta-decarboxylase activity by transamination
    • Novogrodsky, A., Meister, A., Control of aspartate beta-decarboxylase activity by transamination. J. Biol. Chem. 239:3 (1964), 879–888.
    • (1964) J. Biol. Chem. , vol.239 , Issue.3 , pp. 879-888
    • Novogrodsky, A.1    Meister, A.2
  • 55
    • 84963517324 scopus 로고    scopus 로고
    • A synthetic biochemistry module for production of bio-based chemicals from glucose
    • Opgenorth, P.H., Korman, T.P., Bowie, J.U., A synthetic biochemistry module for production of bio-based chemicals from glucose. Nat. Chem. Biol. 12:6 (2016), 393–395, 10.1038/nchembio.2062.
    • (2016) Nat. Chem. Biol. , vol.12 , Issue.6 , pp. 393-395
    • Opgenorth, P.H.1    Korman, T.P.2    Bowie, J.U.3
  • 56
    • 0016302743 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase catalyzed hydration of the 5-6 double bond of reduced β-nicotinamide adenine dinucleotide (β-NADH). Formation of β-6-hydroxy-1,4,5,6-tetrahydronicotinamide adenine dinucleotide
    • Oppenheimer, N.J., Kaplan, N.O., Glyceraldehyde-3-phosphate dehydrogenase catalyzed hydration of the 5-6 double bond of reduced β-nicotinamide adenine dinucleotide (β-NADH). Formation of β-6-hydroxy-1,4,5,6-tetrahydronicotinamide adenine dinucleotide. Biochemistry 13:23 (1974), 4685–4694, 10.1021/bi00720a002.
    • (1974) Biochemistry , vol.13 , Issue.23 , pp. 4685-4694
    • Oppenheimer, N.J.1    Kaplan, N.O.2
  • 57
    • 0015218939 scopus 로고
    • Partial reactions catalyzed by gamma-glutamylcysteine synthetase and evidence for an activated glutamate intermediate
    • Orlowski, M., Meister, A., Partial reactions catalyzed by gamma-glutamylcysteine synthetase and evidence for an activated glutamate intermediate. J. Biol. Chem. 246:23 (1971), 7095–7105.
    • (1971) J. Biol. Chem. , vol.246 , Issue.23 , pp. 7095-7105
    • Orlowski, M.1    Meister, A.2
  • 58
    • 80054069179 scopus 로고    scopus 로고
    • A comprehensive genome-scale reconstruction of Escherichia coli metabolism – 2011
    • Orth, J.D., Conrad, T.M., Na, J., Lerman, J.A., Nam, H., Feist, A.M., Palsson, B.Ø., A comprehensive genome-scale reconstruction of Escherichia coli metabolism – 2011. Mol. Syst. Biol., 7, 2011, 535, 10.1038/msb.2011.65.
    • (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.Ø.7
  • 59
    • 0035433143 scopus 로고    scopus 로고
    • L-Pyroglutamate spontaneously formed from L-glutamate inhibits growth of the hyperthermophilic archaeon Sulfolobus solfataricus
    • Park, C.B., Lee, S.B., Ryu, D.D., L-Pyroglutamate spontaneously formed from L-glutamate inhibits growth of the hyperthermophilic archaeon Sulfolobus solfataricus. Appl. Environ. Microbiol. 67:8 (2001), 3650–3654, 10.1128/AEM.67.8.3650-3654.2001.
    • (2001) Appl. Environ. Microbiol. , vol.67 , Issue.8 , pp. 3650-3654
    • Park, C.B.1    Lee, S.B.2    Ryu, D.D.3
  • 61
    • 85012054620 scopus 로고    scopus 로고
    • The impact of non-enzymatic reactions and enzyme promiscuity on cellular metabolism during (oxidative) stress conditions
    • Piedrafita, G., Keller, M.A., Ralser, M., The impact of non-enzymatic reactions and enzyme promiscuity on cellular metabolism during (oxidative) stress conditions. Biomolecules 5:3 (2015), 2101–2122, 10.3390/biom5032101.
    • (2015) Biomolecules , vol.5 , Issue.3 , pp. 2101-2122
    • Piedrafita, G.1    Keller, M.A.2    Ralser, M.3
  • 63
    • 84895071963 scopus 로고    scopus 로고
    • EC-BLAST: a tool to automatically search and compare enzyme reactions
    • Rahman, S.A., Cuesta, S.M., Furnham, N., Holliday, G.L., Thornton, J.M., EC-BLAST: a tool to automatically search and compare enzyme reactions. Nat. Methods 11:2 (2014), 171–174, 10.1038/nmeth.2803.
    • (2014) Nat. Methods , vol.11 , Issue.2 , pp. 171-174
    • Rahman, S.A.1    Cuesta, S.M.2    Furnham, N.3    Holliday, G.L.4    Thornton, J.M.5
  • 64
    • 0027286747 scopus 로고
    • Mechanism for the formation of methylglyoxal from triosephosphates
    • Richard, J.P., Mechanism for the formation of methylglyoxal from triosephosphates. Biochem. Soc. Trans. 21:2 (1993), 549–553, 10.1042/bst0210549.
    • (1993) Biochem. Soc. Trans. , vol.21 , Issue.2 , pp. 549-553
    • Richard, J.P.1
  • 67
    • 84922264295 scopus 로고    scopus 로고
    • Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues
    • Richarme, G., Mihoub, M., Dairou, J., Bui, L.C., Leger, T., Lamouri, A., Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290:3 (2015), 1885–1897, 10.1074/jbc.M114.597815.
    • (2015) J. Biol. Chem. , vol.290 , Issue.3 , pp. 1885-1897
    • Richarme, G.1    Mihoub, M.2    Dairou, J.3    Bui, L.C.4    Leger, T.5    Lamouri, A.6
  • 68
    • 84871923710 scopus 로고    scopus 로고
    • Analysis of seven folates in food by LC–MS/MS to improve accuracy of total folate data
    • Ringling, C., Rychlik, M., Analysis of seven folates in food by LC–MS/MS to improve accuracy of total folate data. Eur. Food Res. Technol. 236:1 (2013), 17–28, 10.1007/s00217-012-1849-x.
    • (2013) Eur. Food Res. Technol. , vol.236 , Issue.1 , pp. 17-28
    • Ringling, C.1    Rychlik, M.2
  • 69
    • 27944467233 scopus 로고    scopus 로고
    • The gene mutated in L-2-hydroxyglutaric aciduria encodes L-2-hydroxyglutarate dehydrogenase
    • Rzem, R., Van Schaftingen, E., Veiga-da-Cunha, M., The gene mutated in L-2-hydroxyglutaric aciduria encodes L-2-hydroxyglutarate dehydrogenase. Biochimie 88:1 (2006), 113–116, 10.1016/j.biochi.2005.06.005.
    • (2006) Biochimie , vol.88 , Issue.1 , pp. 113-116
    • Rzem, R.1    Van Schaftingen, E.2    Veiga-da-Cunha, M.3
  • 71
    • 34547676311 scopus 로고    scopus 로고
    • Optimization based automated curation of metabolic reconstructions
    • Satish Kumar, V., Dasika, M.S., Maranas, C.D., Optimization based automated curation of metabolic reconstructions. BMC Bioinform., 8, 2007, 212, 10.1186/1471-2105-8-212.
    • (2007) BMC Bioinform. , vol.8 , pp. 212
    • Satish Kumar, V.1    Dasika, M.S.2    Maranas, C.D.3
  • 72
    • 84995955849 scopus 로고    scopus 로고
    • A synthetic pathway for the fixation of carbon dioxide in vitro
    • Schwander, T., Schada von Borzyskowski, L., Burgener, S., Cortina, N.S., Erb, T.J., A synthetic pathway for the fixation of carbon dioxide in vitro. Science 354:6314 (2016), 900–904, 10.1126/science.aah5237.
    • (2016) Science , vol.354 , Issue.6314 , pp. 900-904
    • Schwander, T.1    Schada von Borzyskowski, L.2    Burgener, S.3    Cortina, N.S.4    Erb, T.J.5
  • 74
    • 85012295540 scopus 로고    scopus 로고
    • Epimetabolites: discovering metabolism beyond building and burning
    • Showalter, M.R., Cajka, T., Fiehn, O., Epimetabolites: discovering metabolism beyond building and burning. Curr. Opin. Chem. Biol., 2017, 10.1016/j.cbpa.2017.01.012.
    • (2017) Curr. Opin. Chem. Biol.
    • Showalter, M.R.1    Cajka, T.2    Fiehn, O.3
  • 75
    • 84898944307 scopus 로고    scopus 로고
    • Synthetic metabolons for metabolic engineering
    • Singleton, C., Howard, T.P., Smirnoff, N., Synthetic metabolons for metabolic engineering. J. Exp. Bot. 65:8 (2014), 1947–1954, 10.1093/jxb/eru050.
    • (2014) J. Exp. Bot. , vol.65 , Issue.8 , pp. 1947-1954
    • Singleton, C.1    Howard, T.P.2    Smirnoff, N.3
  • 76
    • 85020239251 scopus 로고    scopus 로고
    • ReactPRED: a tool to predict and analyze biochemical reactions
    • Sivakumar, T.V., Giri, V., Park, J.H., Kim, T.Y., Bhaduri, A., ReactPRED: a tool to predict and analyze biochemical reactions. Bioinformatics 32:22 (2016), 3522–3524, 10.1093/bioinformatics/btw491.
    • (2016) Bioinformatics , vol.32 , Issue.22 , pp. 3522-3524
    • Sivakumar, T.V.1    Giri, V.2    Park, J.H.3    Kim, T.Y.4    Bhaduri, A.5
  • 77
    • 84925491433 scopus 로고    scopus 로고
    • Unlocking the diversity of alkaloids in Catharanthus roseus: nuclear localization suggests metabolic channeling in secondary metabolism
    • Stavrinides, A., Tatsis, E.C., Foureau, E., Caputi, L., Kellner, F., Courdavault, V., O'Connor, S.E., Unlocking the diversity of alkaloids in Catharanthus roseus: nuclear localization suggests metabolic channeling in secondary metabolism. Chem. Biol. 22:3 (2015), 336–341, 10.1016/j.chembiol.2015.02.006.
    • (2015) Chem. Biol. , vol.22 , Issue.3 , pp. 336-341
    • Stavrinides, A.1    Tatsis, E.C.2    Foureau, E.3    Caputi, L.4    Kellner, F.5    Courdavault, V.6    O'Connor, S.E.7
  • 78
    • 0025160752 scopus 로고
    • Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate
    • Stover, P., Schirch, V., Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate. J. Biol. Chem. 265:24 (1990), 14227–14233.
    • (1990) J. Biol. Chem. , vol.265 , Issue.24 , pp. 14227-14233
    • Stover, P.1    Schirch, V.2
  • 79
    • 0027513805 scopus 로고
    • The metabolic role of leucovorin
    • Stover, P., Schirch, V., The metabolic role of leucovorin. Trends Biochem. Sci. 18:3 (1993), 102–106, 10.1016/0968-0004(93)90162-G.
    • (1993) Trends Biochem. Sci. , vol.18 , Issue.3 , pp. 102-106
    • Stover, P.1    Schirch, V.2
  • 82
    • 84902670142 scopus 로고    scopus 로고
    • Accuracy-rate tradeoffs: how do enzymes meet demands of selectivity and catalytic efficiency?
    • Tawfik, D.S., Accuracy-rate tradeoffs: how do enzymes meet demands of selectivity and catalytic efficiency?. Curr. Opin. Chem. Biol. 21 (2014), 73–80, 10.1016/j.cbpa.2014.05.008.
    • (2014) Curr. Opin. Chem. Biol. , vol.21 , pp. 73-80
    • Tawfik, D.S.1
  • 83
    • 43449094351 scopus 로고    scopus 로고
    • Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems. Role in ageing and disease
    • Thornalley, P.J., Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems. Role in ageing and disease. Drug Metabol. Drug Interact. 23:1–2 (2008), 125–150, 10.1515/DMDI.2008.23.1-2.125.
    • (2008) Drug Metabol. Drug Interact. , vol.23 , Issue.1-2 , pp. 125-150
    • Thornalley, P.J.1
  • 84
    • 0025298551 scopus 로고
    • The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley, P.J., The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269:1 (1990), 1–11, 10.1042/bj2690001.
    • (1990) Biochem. J. , vol.269 , Issue.1 , pp. 1-11
    • Thornalley, P.J.1
  • 85
    • 84896930134 scopus 로고    scopus 로고
    • Assay of methylglyoxal and glyoxal and control of peroxidase interference
    • Thornalley, P.J., Rabbani, N., Assay of methylglyoxal and glyoxal and control of peroxidase interference. Biochem. Soc. Trans. 42:2 (2014), 504–510, 10.1042/BST20140009.
    • (2014) Biochem. Soc. Trans. , vol.42 , Issue.2 , pp. 504-510
    • Thornalley, P.J.1    Rabbani, N.2
  • 86
    • 0025786724 scopus 로고
    • 1,3-Propanediol production by Escherichia coli expressing genes from the Klebsiella pneumoniae dha regulon
    • Tong, I.T., Liao, H.H., Cameron, D.C., 1,3-Propanediol production by Escherichia coli expressing genes from the Klebsiella pneumoniae dha regulon. Appl. Environ. Microbiol. 57:12 (1991), 3541–3546.
    • (1991) Appl. Environ. Microbiol. , vol.57 , Issue.12 , pp. 3541-3546
    • Tong, I.T.1    Liao, H.H.2    Cameron, D.C.3
  • 87
    • 0000409606 scopus 로고
    • Spontaneous decomposition of glutamine in cell culture media
    • Tritsch, G.L., Moore, G.E., Spontaneous decomposition of glutamine in cell culture media. Exp. Cell. Res. 28:2 (1962), 360–364, 10.1016/0014-4827(62)90290-2.
    • (1962) Exp. Cell. Res. , vol.28 , Issue.2 , pp. 360-364
    • Tritsch, G.L.1    Moore, G.E.2
  • 88
    • 34548605361 scopus 로고    scopus 로고
    • Microbial metabolomics: toward a platform with full metabolome coverage
    • Van der Werf, M.J., Overkamp, K.M., Muilwijk, B., Coulier, L., Hankemeier, T., Microbial metabolomics: toward a platform with full metabolome coverage. Anal. Biochem. 370:1 (2007), 17–25, 10.1016/j.ab.2007.07.022.
    • (2007) Anal. Biochem. , vol.370 , Issue.1 , pp. 17-25
    • Van der Werf, M.J.1    Overkamp, K.M.2    Muilwijk, B.3    Coulier, L.4    Hankemeier, T.5
  • 89
    • 0015165324 scopus 로고
    • Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate) to L-glutamate coupled with cleavage of adenosine triphosphate to adenosine diphosphate, a reaction in the γ-glutamyl cycle
    • Van der Werf, P., Orlowski, M., Meister, A., Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate) to L-glutamate coupled with cleavage of adenosine triphosphate to adenosine diphosphate, a reaction in the γ-glutamyl cycle. Proc. Natl. Acad. Sci. USA 68:12 (1971), 2982–2985.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , Issue.12 , pp. 2982-2985
    • Van der Werf, P.1    Orlowski, M.2    Meister, A.3
  • 92
    • 64449084807 scopus 로고    scopus 로고
    • L-2-Hydroxyglutaric aciduria, a disorder of metabolite repair
    • Van Schaftingen, E., Rzem, R., Veiga-da-Cunha, M., L-2-Hydroxyglutaric aciduria, a disorder of metabolite repair. J. Inherit. Metab. Dis. 32:2 (2009), 135–142, 10.1007/s10545-008-1042-3.
    • (2009) J. Inherit. Metab. Dis. , vol.32 , Issue.2 , pp. 135-142
    • Van Schaftingen, E.1    Rzem, R.2    Veiga-da-Cunha, M.3
  • 93
    • 84976872328 scopus 로고    scopus 로고
    • enviPath – The environmental contaminant biotransformation pathway resource
    • Wicker, J., Lorsbach, T., Gütlein, M., Schmid, E., Latino, D., Kramer, S., Fenner, K., enviPath – The environmental contaminant biotransformation pathway resource. Nucleic Acids Res. 44:D1 (2016), D502–D508, 10.1093/nar/gkv1229.
    • (2016) Nucleic Acids Res. , vol.44 , Issue.D1 , pp. D502-D508
    • Wicker, J.1    Lorsbach, T.2    Gütlein, M.3    Schmid, E.4    Latino, D.5    Kramer, S.6    Fenner, K.7
  • 94
    • 38849088680 scopus 로고    scopus 로고
    • Identification of proteins involved in formaldehyde metabolism by Rhodobacter sphaeroides
    • Wilson, S.M., Gleisten, M.P., Donohue, T.J., Identification of proteins involved in formaldehyde metabolism by Rhodobacter sphaeroides. Microbiology 154:1 (2008), 296–305, 10.1099/mic.0.2007/011346-0.
    • (2008) Microbiology , vol.154 , Issue.1 , pp. 296-305
    • Wilson, S.M.1    Gleisten, M.P.2    Donohue, T.J.3
  • 95
    • 35148889024 scopus 로고    scopus 로고
    • Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity
    • Withers, S.T., Gottlieb, S.S., Lieu, B., Newman, J.D., Keasling, J.D., Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity. Appl. Environ. Microbiol. 73:19 (2007), 6277–6283, 10.1128/AEM.00861-07.
    • (2007) Appl. Environ. Microbiol. , vol.73 , Issue.19 , pp. 6277-6283
    • Withers, S.T.1    Gottlieb, S.S.2    Lieu, B.3    Newman, J.D.4    Keasling, J.D.5
  • 97
    • 0016683581 scopus 로고
    • Inhibition of NADP-dependent dehydrogenases by modified products of NADPH
    • Yoshida, A., Dave, V., Inhibition of NADP-dependent dehydrogenases by modified products of NADPH. Arch. Biochem. Biophys. 169:1 (1975), 298–303, 10.1016/0003-9861(75)90344-6.
    • (1975) Arch. Biochem. Biophys. , vol.169 , Issue.1 , pp. 298-303
    • Yoshida, A.1    Dave, V.2
  • 99
    • 84876673237 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for high-specificity production of isoprenol and prenol as next generation of biofuels
    • Zheng, Y., Liu, Q., Li, L., Qin, W., Yang, J., Zhang, H., Jiang, X., Cheng, T., Liu, W., Xu, X., Xian, M., Metabolic engineering of Escherichia coli for high-specificity production of isoprenol and prenol as next generation of biofuels. Biotechnol. Biofuels, 6, 2013, 57, 10.1186/1754-6834-6-57.
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 57
    • Zheng, Y.1    Liu, Q.2    Li, L.3    Qin, W.4    Yang, J.5    Zhang, H.6    Jiang, X.7    Cheng, T.8    Liu, W.9    Xu, X.10    Xian, M.11
  • 100
    • 0034878313 scopus 로고    scopus 로고
    • Accumulation of methylglyoxal in anaerobically grown Escherichia coli and its detoxification by expression of the Pseudomonas putida glyoxalase I gene
    • Zhu, M.M., Skraly, F.A., Cameron, D.C., Accumulation of methylglyoxal in anaerobically grown Escherichia coli and its detoxification by expression of the Pseudomonas putida glyoxalase I gene. Metab. Eng. 3:3 (2001), 218–225, 10.1006/mben.2001.0186.
    • (2001) Metab. Eng. , vol.3 , Issue.3 , pp. 218-225
    • Zhu, M.M.1    Skraly, F.A.2    Cameron, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.