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Volumn 97, Issue 18, 2013, Pages 8139-8149

Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum

Author keywords

aroE; Aromatic compound; Corynebacterium glutamicum; Dehydrogenase; Quinate; Shikimate

Indexed keywords

AROE; CORYNEBACTERIUM GLUTAMICUM; DEHYDROGENASE; QUINATE; SHIKIMATES;

EID: 84883555876     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4659-y     Document Type: Article
Times cited : (30)

References (37)
  • 1
    • 0024286625 scopus 로고
    • Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase
    • 3277621 1:CAS:528:DyaL1cXhvVWjtLw%3D
    • Anton IA, Coggins JR (1988) Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem J 249:319-326
    • (1988) Biochem J , vol.249 , pp. 319-326
    • Anton, I.A.1    Coggins, J.R.2
  • 2
    • 0015219583 scopus 로고
    • Kinetic and isotope-exchange studies on shikimate dehydrogenase from Pisum sativum
    • 4397925 10.1021/bi00786a032 1:STN:280:DyaE3M3msFWrtw%3D%3D
    • Balinsky D, Dennis AW, Cleland WW (1971) Kinetic and isotope-exchange studies on shikimate dehydrogenase from Pisum sativum. Biochemistry 10:1947-1952
    • (1971) Biochemistry , vol.10 , pp. 1947-1952
    • Balinsky, D.1    Dennis, A.W.2    Cleland, W.W.3
  • 3
    • 0038820015 scopus 로고    scopus 로고
    • The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase
    • DOI 10.1074/jbc.M301348200
    • Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF (2003) The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J Biol Chem 278:19176-19182 (Pubitemid 36799308)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 19176-19182
    • Benach, J.1    Lee, I.2    Edstrom, W.3    Kuzin, A.P.4    Chiang, Y.5    Acton, T.B.6    Montelione, G.T.7    Hunt, J.F.8
  • 4
    • 0035209901 scopus 로고    scopus 로고
    • Metabolic engineering for microbial production of aromatic amino acids and derived compounds
    • DOI 10.1006/mben.2001.0196
    • Bongaerts J, Krämer M, Müller U, Raeven L, Wubbolts M (2001) Metabolic engineering for microbial production of aromatic amino acids and derived compounds. Metab Eng 3:289-300 (Pubitemid 33136381)
    • (2001) Metabolic Engineering , vol.3 , Issue.4 , pp. 289-300
    • Bongaerts, J.1    Kramer, M.2    Muller, U.3    Raeven, L.4    Wubbolts, M.5
  • 5
    • 0027965624 scopus 로고
    • Cloning of cDNA encoding the bifunctional dehydroquinase·shikimate dehydrogenase of aromatic-amino-acid biosynthesis in Nicotiana tabacum
    • Bonner CA, Jensen RA (1994) Cloning of cDNA encoding the bifunctional dehydroquinase.shikimate dehydrogenase of aromatic-amino-acid biosynthesis in Nicotiana tabacum. Biochem J 302:11-14 (Pubitemid 24256329)
    • (1994) Biochemical Journal , vol.302 , Issue.1 , pp. 11-14
    • Bonner, C.A.1    Jensen, R.A.2
  • 6
    • 0022425494 scopus 로고
    • The purification of shikimate dehydrogenase from Escherichia coli
    • 3883995 1:CAS:528:DyaL2MXhtVylsbc%3D
    • Chaudhuri S, Coggins JR (1985) The purification of shikimate dehydrogenase from Escherichia coli. Biochem J 226:217-223
    • (1985) Biochem J , vol.226 , pp. 217-223
    • Chaudhuri, S.1    Coggins, J.R.2
  • 7
    • 0027772102 scopus 로고
    • Identification and removal of impediments to biocatalytic synthesis of aromatics from D-glucose: Rate-limiting enzymes in the common pathway of aromatic amino acid biosynthesis
    • DOI 10.1021/ja00077a065
    • Dell KA, Frost JW (1993) Identification and removal of impediments to biocatalytic synthesis of aromatics from d-glucose: rate-limiting enzymes in the common pathway of aromatic amino acid biosynthesis. J Am Chem Soc 115:11581-11589 (Pubitemid 24017370)
    • (1993) Journal of the American Chemical Society , vol.115 , Issue.24 , pp. 11581-11589
    • Dell, K.A.1    Frost, J.W.2
  • 8
    • 0023414737 scopus 로고
    • The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains
    • 2825635 1:CAS:528:DyaL1cXltF2msA%3D%3D
    • Duncan K, Edwards RM, Coggins JR (1987) The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains. Biochem J 246:375-386
    • (1987) Biochem J , vol.246 , pp. 375-386
    • Duncan, K.1    Edwards, R.M.2    Coggins, J.R.3
  • 9
    • 67650543834 scopus 로고    scopus 로고
    • Regulation of quinone oxidoreductase by the redox-sensing transcriptional regulator QorR in Corynebacterium glutamicum
    • 19403527 10.1074/jbc.M109.009027 1:CAS:528:DC%2BD1MXntFCjs7c%3D
    • Ehira S, Ogino H, Teramoto H, Inui M, Yukawa H (2009) Regulation of quinone oxidoreductase by the redox-sensing transcriptional regulator QorR in Corynebacterium glutamicum. J Biol Chem 284:16736-16742
    • (2009) J Biol Chem , vol.284 , pp. 16736-16742
    • Ehira, S.1    Ogino, H.2    Teramoto, H.3    Inui, M.4    Yukawa, H.5
  • 10
    • 74549157678 scopus 로고    scopus 로고
    • Functional genomics of pH homeostasis in Corynebacterium glutamicum revealed novel links between pH response, oxidative stress, iron homeostasis and methionine synthesis
    • 20025733 10.1186/1471-2164-10-621
    • Follmann M, Ochrombel I, Krämer R, Trötschel C, Poetsch A, Rückert C, Hüser A, Persicke M, Seiferling D, Kalinowski J, Marin K (2009) Functional genomics of pH homeostasis in Corynebacterium glutamicum revealed novel links between pH response, oxidative stress, iron homeostasis and methionine synthesis. BMC Genomics 10:621
    • (2009) BMC Genomics , vol.10 , pp. 621
    • Follmann, M.1    Ochrombel, I.2    Krämer, R.3    Trötschel, C.4    Poetsch, A.5    Rückert, C.6    Hüser, A.7    Persicke, M.8    Seiferling, D.9    Kalinowski, J.10    Marin, K.11
  • 13
    • 33749396618 scopus 로고    scopus 로고
    • Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori
    • DOI 10.1111/j.1742-4658.2006.05469.x
    • Han C, Wang L, Yu K, Chen L, Hu L, Chen K, Jiang H, Shen X (2006) Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori. FEBS J 273:4682-4692 (Pubitemid 44506909)
    • (2006) FEBS Journal , vol.273 , Issue.20 , pp. 4682-4692
    • Han, C.1    Wang, L.2    Yu, K.3    Chen, L.4    Hu, L.5    Chen, K.6    Jiang, H.7    Shen, X.8
  • 14
    • 0041429540 scopus 로고    scopus 로고
    • Industrial production of amino acids by coryneform bacteria
    • DOI 10.1016/S0168-1656(03)00149-4
    • Hermann T (2003) Industrial production of amino acids by coryneform bacteria. J Biotechnol 104:155-172 (Pubitemid 37011355)
    • (2003) Journal of Biotechnology , vol.104 , Issue.1-3 , pp. 155-172
    • Hermann, T.1
  • 16
    • 0028406892 scopus 로고
    • Fermentative production of tryptophan by a stable recombinant strain of Corynebacterium glutamicum with a modified serine-biosynthetic pathway
    • Ikeda M, Nakanishi K, Kino K, Katsumata R (1994) Fermentative production of tryptophan by a stable recombinant strain of Corynebacterium glutamicum with a modified serine-biosynthetic pathway. Biosci Biotechnol Biochem 58:674-678 (Pubitemid 2096175)
    • (1994) Bioscience, Biotechnology and Biochemistry , vol.58 , Issue.4 , pp. 674-678
    • Ikeda, M.1    Nakanishi, K.2    Kino, K.3    Katsumata, R.4
  • 17
    • 0033009718 scopus 로고    scopus 로고
    • Hyperproduction of tryptophan by Corynebacterium glutamicum with the modified pentose phosphate pathway
    • 10347033 1:CAS:528:DyaK1MXjs12gsbo%3D
    • Ikeda M, Katsumata R (1999) Hyperproduction of tryptophan by Corynebacterium glutamicum with the modified pentose phosphate pathway. Appl Environ Microbiol 65:2497-2502
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2497-2502
    • Ikeda, M.1    Katsumata, R.2
  • 18
  • 19
    • 0031001311 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of phenylalanine-sensitive 3- deoxy-d-arabino-heptulosonate-7-phosphate synthase of Escherichia coli
    • Kikuchi Y, Tsujimoto K, Kurahashi O (1997) Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-d-arabino-heptulosonate-7- phosphate synthase of Escherichia coli. Appl Environ Microbiol 63:761-762 (Pubitemid 27121565)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.2 , pp. 761-762
    • Kikuchi, Y.1    Tsujimoto, K.2    Kurahashi, O.3
  • 20
    • 0023896661 scopus 로고
    • Amino acid biosynthesis inhibitors as herbicides
    • 3052285 10.1146/annurev.bi.57.070188.003211 1:CAS:528:DyaL1cXkvVyjsLs%3D
    • Kishore GM, Shah DM (1988) Amino acid biosynthesis inhibitors as herbicides. Annu Rev Biochem 57:627-663
    • (1988) Annu Rev Biochem , vol.57 , pp. 627-663
    • Kishore, G.M.1    Shah, D.M.2
  • 21
    • 0037321888 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • DOI 10.1039/b100399m
    • Knaggs AR (2003) The biosynthesis of shikimate metabolites. Nat Prod Rep 20:119-136 (Pubitemid 36219435)
    • (2003) Natural Product Reports , vol.20 , Issue.1 , pp. 119-136
    • Knaggs, A.R.1
  • 22
    • 84866285573 scopus 로고    scopus 로고
    • Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway
    • 22752168 10.1128/AEM.01148-12 1:CAS:528:DC%2BC38Xht1Giu7zM
    • Koma D, Yamanaka H, Moriyoshi K, Ohmoto T, Sakai K (2012) Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway. Appl Environ Microbiol 78:6203-6216
    • (2012) Appl Environ Microbiol , vol.78 , pp. 6203-6216
    • Koma, D.1    Yamanaka, H.2    Moriyoshi, K.3    Ohmoto, T.4    Sakai, K.5
  • 23
    • 0017619442 scopus 로고
    • The subunit structure of the arom multienzyme complex of Neurospora crassa. A possible pentafunctional polypeptide chain
    • Lumsden J, Coggins JR (1977) The subunit structure of the arom multienzyme complex of Neurospora crassa. A possible pentafunctional polypeptide chain. Biochem J 161:599-607 (Pubitemid 8047339)
    • (1977) Biochemical Journal , vol.161 , Issue.3 , pp. 599-607
    • Lumsden, J.1    Coggins, J.R.2
  • 24
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • 19047729 10.1099/mic.0.2008/022772-0 1:CAS:528:DC%2BD1MXhsVCjsg%3D%3D
    • Maddocks SE, Oyston PC (2008) Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154:3609-3623
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 25
  • 26
    • 0024255488 scopus 로고
    • Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase of Escherichia coli
    • 2903857 1:CAS:528:DyaL1MXkslajs7o%3D
    • Ray JM, Yanofsky C, Bauerle R (1988) Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-d-arabino-heptulosonate- 7-phosphate synthase of Escherichia coli. J Bacteriol 170:5500-5506
    • (1988) J Bacteriol , vol.170 , pp. 5500-5506
    • Ray, J.M.1    Yanofsky, C.2    Bauerle, R.3
  • 27
    • 33748857142 scopus 로고    scopus 로고
    • Evolutionary origins of the eukaryotic shikimate pathway: Gene fusions, horizontal gene transfer, and endosymbiotic replacements
    • DOI 10.1128/EC.00106-06
    • Richards TA, Dacks JB, Campbell SA, Blanchard JL, Foster PG, McLeod R, Roberts CW (2006) Evolutionary origins of the eukaryotic shikimate pathway: gene fusions, horizontal gene transfer, and endosymbiotic replacements. Eukaryot Cell 5:1517-1531 (Pubitemid 44423648)
    • (2006) Eukaryotic Cell , vol.5 , Issue.9 , pp. 1517-1531
    • Richards, T.A.1    Dacks, J.B.2    Campbell, S.A.3    Blanchard, J.L.4    Foster, P.G.5    McLeod, R.6    Roberts, C.W.7
  • 30
    • 52449083936 scopus 로고    scopus 로고
    • A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass
    • 18669580 10.1093/molbev/msn170 1:CAS:528:DC%2BD1cXht1ektbnJ
    • Singh S, Stavrinides J, Christendat D, Guttman DS (2008) A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol Biol Evol 25:2221-2232
    • (2008) Mol Biol Evol , vol.25 , pp. 2221-2232
    • Singh, S.1    Stavrinides, J.2    Christendat, D.3    Guttman, D.S.4
  • 31
    • 38649138543 scopus 로고    scopus 로고
    • Regulation of the expression of phosphoenolpyruvate: Carbohydrate phosphotransferase system (PTS) genes in Corynebacterium glutamicum R
    • DOI 10.1099/mic.0.2007/008862-0
    • Tanaka Y, Okai N, Teramoto H, Inui M, Yukawa H (2008) Regulation of the expression of phosphoenolpyruvate: Carbohydrate phosphotransferase system (PTS) genes in Corynebacterium glutamicum R. Microbiology 154:264-274 (Pubitemid 351201406)
    • (2008) Microbiology , vol.154 , Issue.1 , pp. 264-274
    • Tanaka, Y.1    Okai, N.2    Teramoto, H.3    Inui, M.4    Yukawa, H.5
  • 32
    • 66249138103 scopus 로고    scopus 로고
    • Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum
    • 19376919 10.1128/AEM.00163-09 1:CAS:528:DC%2BD1MXntlShurw%3D
    • Teramoto H, Inui M, Yukawa H (2009) Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. Appl Environ Microbiol 75:3461-3468
    • (2009) Appl Environ Microbiol , vol.75 , pp. 3461-3468
    • Teramoto, H.1    Inui, M.2    Yukawa, H.3
  • 33
    • 0025016270 scopus 로고
    • Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-arabino-heptuloxsonate 7-phosphate synthase
    • Weaver LM, Herrmann KM (1990) Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J Bacteriol 172:6581-6584 (Pubitemid 20372805)
    • (1990) Journal of Bacteriology , vol.172 , Issue.11 , pp. 6581-6584
    • Weaver, L.M.1    Herrmann, K.M.2
  • 34
    • 0038154081 scopus 로고    scopus 로고
    • The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
    • DOI 10.1128/JB.185.14.4144-4151.2003
    • Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE (2003) The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J Bacteriol 185:4144-4151 (Pubitemid 36835254)
    • (2003) Journal of Bacteriology , vol.185 , Issue.14 , pp. 4144-4151
    • Ye, S.1    Von Delft, F.2    Brooun, A.3    Knuth, M.W.4    Swanson, R.V.5    McRee, D.E.6
  • 35
    • 0035918169 scopus 로고    scopus 로고
    • Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in Amycolatopsis mediterranei S699
    • 11278540 10.1074/jbc.M009667200 1:CAS:528:DC%2BD3MXjtFyntrY%3D
    • Yu TW, Müller R, Müller M, Zhang X, Draeger G, Kim CG, Leistner E, Floss HG (2001) Mutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid, the starter unit of rifamycin biosynthesis in Amycolatopsis mediterranei S699. J Biol Chem 276:12546-12555
    • (2001) J Biol Chem , vol.276 , pp. 12546-12555
    • Yu, T.W.1    Müller, R.2    Müller, M.3    Zhang, X.4    Draeger, G.5    Kim, C.G.6    Leistner, E.7    Floss, H.G.8


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