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Volumn 28, Issue 16, 2006, Pages 1227-1232

Cloning, expression and characterization of a thiolase gene from Clostridium pasteurianum

Author keywords

Clostridium pasteurianum; Thiolase purification; thl gene cloning; thl overexpression

Indexed keywords

CLOSTRIDIUM PASTEURIANUM; THIOLASE PURIFICATION; THL GENE CLONING; THL OVEREXPRESSION;

EID: 33746079588     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-006-9089-4     Document Type: Article
Times cited : (8)

References (19)
  • 1
    • 0016610692 scopus 로고
    • Kinetics and properties of beta-ketothiolase from Clostridium pasteurianum
    • Berndt H, Schlegel HG (1975) Kinetics and properties of beta-ketothiolase from Clostridium pasteurianum. Arch Microbiol 103:21-30
    • (1975) Arch Microbiol , vol.103 , pp. 21-30
    • Berndt, H.1    Schlegel, H.G.2
  • 2
    • 0034790655 scopus 로고    scopus 로고
    • Fermentation of glycerol by Clostridium pasteurianum - Batch and continuous culture studies
    • Biebl H (2001) Fermentation of glycerol by Clostridium pasteurianum - batch and continuous culture studies. J Ind Microbiol Biotechnol 27:18-26
    • (2001) J Ind Microbiol Biotechnol , vol.27 , pp. 18-26
    • Biebl, H.1
  • 4
    • 0023089497 scopus 로고
    • Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: The ato system
    • Jenkins LS, Nunn WD (1987) Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system. J Bacteriol 169:42-52
    • (1987) J Bacteriol , vol.169 , pp. 42-52
    • Jenkins, L.S.1    Nunn, W.D.2
  • 5
    • 0037207126 scopus 로고    scopus 로고
    • The catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes
    • Kursula P, Ojala J, Lambeir AM, Wierenga RK (2002) The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Biochemistry 41:15543-15556
    • (2002) Biochemistry , vol.41 , pp. 15543-15556
    • Kursula, P.1    Ojala, J.2    Lambeir, A.M.3    Wierenga, R.K.4
  • 6
    • 0032485354 scopus 로고    scopus 로고
    • Metabolic modeling of polyhydroxybutyrate biosynthesis
    • Leaf TA, Srienc F (1998) Metabolic modeling of polyhydroxybutyrate biosynthesis. Biotechnol Bioeng 57:557-570
    • (1998) Biotechnol Bioeng , vol.57 , pp. 557-570
    • Leaf, T.A.1    Srienc, F.2
  • 7
    • 0021102426 scopus 로고
    • Influence of pN2 and pD2 on HD formation by various nitrogenases
    • Li JL, Burris RH (1983) Influence of pN2 and pD2 on HD formation by various nitrogenases. Biochemistry 22:4472-4480
    • (1983) Biochemistry , vol.22 , pp. 4472-4480
    • Li, J.L.1    Burris, R.H.2
  • 8
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu YG, Whittier RF (1995) Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25:674-681
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 9
    • 0014945455 scopus 로고
    • Purification and some properties of thiolase from Escherichia coli
    • Mazzei Y, Negrel R, Ailhaud G (1970) Purification and some properties of thiolase from Escherichia coli. Biochim Biophys Acta 220:129-131
    • (1970) Biochim Biophys Acta , vol.220 , pp. 129-131
    • Mazzei, Y.1    Negrel, R.2    Ailhaud, G.3
  • 10
    • 0033569705 scopus 로고    scopus 로고
    • A biosynthetic thiolase in complex with a reaction intermediate: The crystal structure provides new insights into the catalytic mechanism
    • Modis Y, Wierenga RK (1999) A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism. Structure Fold Des 7:1279-1290
    • (1999) Structure Fold des , vol.7 , pp. 1279-1290
    • Modis, Y.1    Wierenga, R.K.2
  • 11
    • 0034646566 scopus 로고    scopus 로고
    • Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase
    • Modis Y, Wierenga RK (2000) Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase. J Mol Biol 297:1171-1182
    • (2000) J Mol Biol , vol.297 , pp. 1171-1182
    • Modis, Y.1    Wierenga, R.K.2
  • 13
    • 0024445845 scopus 로고
    • Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase
    • Peoples OP, Sinskey AJ (1989) Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase. J Biol Chem 264:15293-15297
    • (1989) J Biol Chem , vol.264 , pp. 15293-15297
    • Peoples, O.P.1    Sinskey, A.J.2
  • 14
    • 0025884710 scopus 로고
    • Cloning of the Clostridium acetobutylicum ATCC 824 acetyl coenzyme A acetyltransferase (thiolase; EC 2.3.1.9) gene
    • Petersen DJ, Bennett GN (1991) Cloning of the Clostridium acetobutylicum ATCC 824 acetyl coenzyme A acetyltransferase (thiolase; EC 2.3.1.9) gene. Appl Environ Microbiol 57:2735-2741
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2735-2741
    • Petersen, D.J.1    Bennett, G.N.2
  • 15
    • 0014010342 scopus 로고
    • The biosynthesis of beta-hydroxy-beta-methylglutaryl coenzyme A in yeast. 3. Purification and properties of the condensing enzyme thiolase system
    • Stewart PR, Rudney H (1966) The biosynthesis of beta-hydroxy-beta- methylglutaryl coenzyme A in yeast. 3. Purification and properties of the condensing enzyme thiolase system. J Biol Chem 241:1212-1221
    • (1966) J Biol Chem , vol.241 , pp. 1212-1221
    • Stewart, P.R.1    Rudney, H.2
  • 16
    • 0024967191 scopus 로고
    • Mechanistic studies on beta-ketoacyl thiolase from Zoogloea ramigera: Identification of the active-site nucleophile as Cys89, its mutation to Ser89, and kinetic and thermodynamic characterization of wild-type and mutant enzymes
    • Thompson S, Mayerl F, Peoples OP, Masamune S, Sinskey AJ, Walsh CT (1989) Mechanistic studies on beta-ketoacyl thiolase from Zoogloea ramigera: identification of the active-site nucleophile as Cys89, its mutation to Ser89, and kinetic and thermodynamic characterization of wild-type and mutant enzymes. Biochemistry 28:5735-5742
    • (1989) Biochemistry , vol.28 , pp. 5735-5742
    • Thompson, S.1    Mayerl, F.2    Peoples, O.P.3    Masamune, S.4    Sinskey, A.J.5    Walsh, C.T.6
  • 17
    • 0026746281 scopus 로고
    • Biosynthetic thiolase from Zoogloea ramigera. Mutagenesis of the putative active-site base Cys-378 to Ser-378 changes the partitioning of the acetyl S-enzyme intermediate
    • Williams SF, Palmer MA, Peoples OP, Walsh CT, Sinskey AJ, Masamune S (1992) Biosynthetic thiolase from Zoogloea ramigera. Mutagenesis of the putative active-site base Cys-378 to Ser-378 changes the partitioning of the acetyl S-enzyme intermediate. J Biol Chem 267:16041-16043
    • (1992) J Biol Chem , vol.267 , pp. 16041-16043
    • Williams, S.F.1    Palmer, M.A.2    Peoples, O.P.3    Walsh, C.T.4    Sinskey, A.J.5    Masamune, S.6
  • 18
    • 0033768632 scopus 로고    scopus 로고
    • Differential regulation of two thiolase genes from Clostridium acetobutylicum DSM 792
    • Winzer K, Lorenz K, Zickner B, Durre P (2000) Differential regulation of two thiolase genes from Clostridium acetobutylicum DSM 792. J Mol Microbiol Biotechnol 2:531-541
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 531-541
    • Winzer, K.1    Lorenz, K.2    Zickner, B.3    Durre, P.4
  • 19
    • 2642579275 scopus 로고    scopus 로고
    • Expression and purification of Histagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins
    • Zeng J, Li D (2004) Expression and purification of Histagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins. Protein Expr Purif 35:320-326
    • (2004) Protein Expr Purif , vol.35 , pp. 320-326
    • Zeng, J.1    Li, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.