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Volumn 4, Issue 1, 2014, Pages 1-8

Disruption of pknG enhances production of gamma-aminobutyric acid by corynebacterium glutamicum expressing glutamate decarboxylase

Author keywords

2 oxoglutarate dehydrogenase; Corynebacterium glutamicum; Gamma aminobutyric acid; Glutamate decarboxylase; Protein kinase G

Indexed keywords

2 OXOGLUTARIC ACID; 4 AMINOBUTYRIC ACID; AMMONIUM SULFATE; BIOTIN; GLUTAMATE DECARBOXYLASE; KANAMYCIN; MAGNESIUM SULFATE; MANGANESE SULFATE; POTASSIUM DIHYDROGEN PHOSPHATE; PROTEIN SERINE THREONINE KINASE; PROTEIN SERINE THREONINE KINASE G; SODIUM CHLORIDE; SUCROSE; THIAMINE; UNCLASSIFIED DRUG; UREA;

EID: 84897119619     PISSN: None     EISSN: 21910855     Source Type: Journal    
DOI: 10.1186/s13568-014-0020-4     Document Type: Article
Times cited : (52)

References (27)
  • 2
    • 77955886345 scopus 로고    scopus 로고
    • Medium optimization for production of gamma-aminobutyric acid by Lactobacillus brevis NCL912
    • Cao YS, Li HX, Qiu T, Gao DD (2010) Medium optimization for production of gamma-aminobutyric acid by Lactobacillus brevis NCL912. Amino Acids 38:1439-1445
    • (2010) Amino Acids , vol.38 , pp. 1439-1445
    • Cao, Y.S.1    Li, H.X.2    Qiu, T.3    Gao, D.D.4
  • 3
    • 0030470440 scopus 로고    scopus 로고
    • Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli
    • DeBiase D, Tramonti A, John RA, Bossa F (1996) Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli. Protein Expr Purif 8:430-438
    • (1996) Protein Expr Purif , vol.8 , pp. 430-438
    • Debiase, D.1    Tramonti, A.2    John, R.A.3    Bossa, F.4
  • 4
    • 0022272437 scopus 로고
    • L-glutamate decarboxylase from bacteria
    • Fonda ML (1985) L-glutamate decarboxylase from bacteria. Methods Enzymol 113:11-16
    • (1985) Methods Enzymol , vol.113 , pp. 11-16
    • Fonda, M.L.1
  • 6
    • 0028765935 scopus 로고
    • Degradation of several polyamides in soils
    • Hashimoto K, Hamano T, Okada M (1994) Degradation of several polyamides in soils. J Appl Polym Sci 54:1579-1583
    • (1994) J Appl Polym Sci , vol.54 , pp. 1579-1583
    • Hashimoto, K.1    Hamano, T.2    Okada, M.3
  • 7
    • 6944223229 scopus 로고    scopus 로고
    • Effect of a gamma-aminobutyric acid-enriched dairy product on the blood pressure of spontaneously hypertensive and normotensive Wistar-Kyoto rats
    • Hayakawa K, Kimura M, Kasaha K, Matsumoto K, Sansawa H, Yamori Y (2004) Effect of a gamma-aminobutyric acid-enriched dairy product on the blood pressure of spontaneously hypertensive and normotensive Wistar-Kyoto rats. Br J Nutr 92:411-417
    • (2004) Br J Nutr , vol.92 , pp. 411-417
    • Hayakawa, K.1    Kimura, M.2    Kasaha, K.3    Matsumoto, K.4    Sansawa, H.5    Yamori, Y.6
  • 8
    • 0041429540 scopus 로고    scopus 로고
    • Industrial production of amino acids by Coryneform bacteria
    • Hermann T (2003) Industrial production of amino acids by Coryneform bacteria. J Biotechnol 104:155-172
    • (2003) J Biotechnol , vol.104 , pp. 155-172
    • Hermann, T.1
  • 9
    • 26844539601 scopus 로고    scopus 로고
    • Synthesis, thermal and mechanical properties and biodegradation of branched polyamide 4
    • Kawasaki N, Nakayama A, Yamano N, Takeda S, Kawata Y, Yamamoto N, Aiba S (2005) Synthesis, thermal and mechanical properties and biodegradation of branched polyamide 4. Polymer 46:9987-9993
    • (2005) Polymer , vol.46 , pp. 9987-9993
    • Kawasaki, N.1    Nakayama, A.2    Yamano, N.3    Takeda, S.4    Kawata, Y.5    Yamamoto, N.6    Aiba, S.7
  • 10
    • 0036965818 scopus 로고    scopus 로고
    • Triggering mechanism of L-glutamate overproduction by dtsR1 in Coryneform bacteria
    • Kimura E (2002) Triggering mechanism of L-glutamate overproduction by dtsR1 in Coryneform bacteria. J Biosci Bioeng 94:545-551
    • (2002) J Biosci Bioeng , vol.94 , pp. 545-551
    • Kimura, E.1
  • 11
    • 28344455644 scopus 로고    scopus 로고
    • Biotechnological production of amino acids and derivatives: Current status and prospects
    • Leuchtenberger W, Huthmacher K, Drauz K (2005) Biotechnological production of amino acids and derivatives: Current status and prospects. Appl Microbiol Biotechnol 69:1-8
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 1-8
    • Leuchtenberger, W.1    Huthmacher, K.2    Drauz, K.3
  • 12
    • 78449276921 scopus 로고    scopus 로고
    • Lactic acid bacterial cell factories for gamma-aminobutyric acid
    • Li HX, Cao YS (2010) Lactic acid bacterial cell factories for gamma-aminobutyric acid. Amino Acids 39:1107-1116
    • (2010) Amino Acids , vol.39 , pp. 1107-1116
    • Li, H.X.1    Cao, Y.S.2
  • 13
    • 42449106500 scopus 로고    scopus 로고
    • Production of gamma-aminobutyric acid by Streptococcus salivarius subsp. thermophilus Y2 under submerged fermentation
    • Lu ZX, Yang SY, Lu FX, Bie XM, Jiao Y, Sun LJ, Yu B (2008) Production of gamma-aminobutyric acid by Streptococcus salivarius subsp. thermophilus Y2 under submerged fermentation. Amino Acids 34:473-478
    • (2008) Amino Acids , vol.34 , pp. 473-478
    • Lu, Z.X.1    Yang, S.Y.2    Lu, F.X.3    Bie, X.M.4    Jiao, Y.5    Sun, L.J.6    Yu, B.7
  • 14
    • 36148935215 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for cadaverine fermentation
    • Mimitsuka T, Sawai H, Hatsu M, Yamada K (2007) Metabolic engineering of Corynebacterium glutamicum for cadaverine fermentation. Biosci Biotechnol Biochem 71:2130-2135
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 2130-2135
    • Mimitsuka, T.1    Sawai, H.2    Hatsu, M.3    Yamada, K.4
  • 15
    • 33744950488 scopus 로고    scopus 로고
    • Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein
    • Niebisch A, Kabus A, Schultz C, Weil B, Bott M (2006) Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein. J Biol Chem 281:12300-12307
    • (2006) J Biol Chem , vol.281 , pp. 12300-12307
    • Niebisch, A.1    Kabus, A.2    Schultz, C.3    Weil, B.4    Bott, M.5
  • 16
    • 45749124318 scopus 로고    scopus 로고
    • Glutamate decarboxylase from Lactobacillus brevis: Activation by ammonium sulfate
    • Oda KH, Hiraga K, Ueno YH (2008) Glutamate decarboxylase from Lactobacillus brevis: Activation by ammonium sulfate. Biosci Biotechnol Biochem 72:1299-1306
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 1299-1306
    • Oda, K.H.1    Hiraga, K.2    Ueno, Y.H.3
  • 17
    • 34548008354 scopus 로고    scopus 로고
    • Glutamate production by Corynebacterium glutamicum: Dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG
    • Schultz C, Niebisch A, Gebel L, Bott M (2007) Glutamate production by Corynebacterium glutamicum: Dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG. Appl Microbiol Biotechnol 76:691-700
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 691-700
    • Schultz, C.1    Niebisch, A.2    Gebel, L.3    Bott, M.4
  • 18
    • 70350423494 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the serine/threonine protein kinases PknA, PknB, PknG and PknL of Corynebacterium glutamicum: Evidence for non-essentiality and for phosphorylation of OdhI and FtsZ by multiple kinases
    • Schultz C, Niebisch A, Schwaiger A, Viets U, Metzger S, Bramkamp M, Bott M (2009) Genetic and biochemical analysis of the serine/threonine protein kinases PknA, PknB, PknG and PknL of Corynebacterium glutamicum: Evidence for non-essentiality and for phosphorylation of OdhI and FtsZ by multiple kinases. Mol Microbiol 74:724-741
    • (2009) Mol Microbiol , vol.74 , pp. 724-741
    • Schultz, C.1    Niebisch, A.2    Schwaiger, A.3    Viets, U.4    Metzger, S.5    Bramkamp, M.6    Bott, M.7
  • 19
    • 84886289603 scopus 로고    scopus 로고
    • Enhancement of gamma-aminobutyric acid production in recombinant Corynebacterium glutamicum by co-expressing two glutamate decarboxylase genes from Lactobacillus brevis
    • Shi F, Jiang J, Li Y, Xie Y (2013) Enhancement of gamma-aminobutyric acid production in recombinant Corynebacterium glutamicum by co-expressing two glutamate decarboxylase genes from Lactobacillus brevis. J Ind Microbiol Biotechnol 40:1285-1296
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 1285-1296
    • Shi, F.1    Jiang, J.2    Li, Y.3    Xie, Y.4
  • 20
    • 0002640894 scopus 로고
    • Effect of biotin on the bacterial formation of glutamic acid I. Glutamate formation and cellular permeability of amino acids
    • Shiio I, Otsuka SI, Takahashi M (1962) Effect of biotin on the bacterial formation of glutamic acid I. Glutamate formation and cellular permeability of amino acids. J Biochem 51:56-62
    • (1962) J Biochem , vol.51 , pp. 56-62
    • Shiio, I.1    Otsuka, S.I.2    Takahashi, M.3
  • 21
    • 18144365501 scopus 로고    scopus 로고
    • Production of gamma-aminobutyric acid (GABA) by Lactobacillus paracasei isolated from traditional fermented foods
    • Shima J, Komatsuzaki N, Kawamoto S, Momose H, Kimura T (2005) Production of gamma-aminobutyric acid (GABA) by Lactobacillus paracasei isolated from traditional fermented foods. Food Microbiol 22:497-504
    • (2005) Food Microbiol , vol.22 , pp. 497-504
    • Shima, J.1    Komatsuzaki, N.2    Kawamoto, S.3    Momose, H.4    Kimura, T.5
  • 22
    • 40449111663 scopus 로고    scopus 로고
    • Characterization of glutamate decarboxylase from a high gamma-aminobutyric acid (GABA)-producer, Lactobacillus paracasei
    • Shima J, Komatsuzaki N, Nakamura T, Kimura T (2008) Characterization of glutamate decarboxylase from a high gamma-aminobutyric acid (GABA)-producer, Lactobacillus paracasei. Biosci Biotechnol Biochem 72:278-285
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 278-285
    • Shima, J.1    Komatsuzaki, N.2    Nakamura, T.3    Kimura, T.4
  • 23
    • 84863100643 scopus 로고    scopus 로고
    • Robust production of gamma-amino butyric acid using recombinant Corynebacterium glutamicum expressing glutamate decarboxylase from Escherichia coli
    • Takahashi C, Shirakawa J, Tsuchidate T, Okai N, Hatada K, Nakayama H, Tateno T, Ogino C, Kondo A (2012) Robust production of gamma-amino butyric acid using recombinant Corynebacterium glutamicum expressing glutamate decarboxylase from Escherichia coli. Enzyme Microb Technol 51:171-176
    • (2012) Enzyme Microb Technol , vol.51 , pp. 171-176
    • Takahashi, C.1    Shirakawa, J.2    Tsuchidate, T.3    Okai, N.4    Hatada, K.5    Nakayama, H.6    Tateno, T.7    Ogino, C.8    Kondo, A.9
  • 24
    • 36248965184 scopus 로고    scopus 로고
    • Direct production of L-lysine from raw corn starch by Corynebacterium glutamicum secreting Streptococcus bovis alpha-amylase using cspB promoter and signal sequence
    • Tateno T, Fukuda H, Kondo A (2007) Direct production of L-lysine from raw corn starch by Corynebacterium glutamicum secreting Streptococcus bovis alpha-amylase using cspB promoter and signal sequence. Appl Microbiol Biotechnol 77:533-541
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 533-541
    • Tateno, T.1    Fukuda, H.2    Kondo, A.3
  • 25
    • 58549095930 scopus 로고    scopus 로고
    • Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylase
    • Tateno T, Okada Y, Tsuchidate T, Tanaka T, Fukuda H, Kondo A (2009) Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylase. Appl Microbiol Biotechnol 82:115-121
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 115-121
    • Tateno, T.1    Okada, Y.2    Tsuchidate, T.3    Tanaka, T.4    Fukuda, H.5    Kondo, A.6
  • 26
    • 79954622477 scopus 로고    scopus 로고
    • Glutamate production from beta-glucan using endoglucanase-secreting Corynebacterium glutamicum
    • Tsuchidate T, Tateno T, Okai N, Tanaka T, Ogino C, Kondo A (2011) Glutamate production from beta-glucan using endoglucanase-secreting Corynebacterium glutamicum. Appl Microbiol Biotechnol 90:895-901
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 895-901
    • Tsuchidate, T.1    Tateno, T.2    Okai, N.3    Tanaka, T.4    Ogino, C.5    Kondo, A.6
  • 27
    • 57749179540 scopus 로고    scopus 로고
    • Mechanism and characterization of polyamide 4 degradation by Pseudomonas sp
    • Yamano N, Nakayama A, Kawasaki N, Yamamoto N, Aiba S (2008) Mechanism and characterization of polyamide 4 degradation by Pseudomonas sp. J Polym Environ 16:141-146
    • (2008) J Polym Environ , vol.16 , pp. 141-146
    • Yamano, N.1    Nakayama, A.2    Kawasaki, N.3    Yamamoto, N.4    Aiba, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.