메뉴 건너뛰기




Volumn 79, Issue 19, 2013, Pages 6134-6139

Directed evolution and structural analysis of nadph-dependent acetoacetyl coenzyme A(acetoacetyl-CoA) reductase from ralstonia eutropha reveals two mutations responsible for enhanced kinetics

Author keywords

[No Author keywords available]

Indexed keywords

CORYNEBACTERIUM GLUTAMICUM; CRYSTAL STRUCTURE DATA; DIRECTED EVOLUTION; POLY-3-HYDROXYBUTYRATE; POLYHYDROXYALKANOATE SYNTHASE; RALSTONIA EUTROPHA; SUBSTRATE RECOGNITION; WILD-TYPE ENZYMES;

EID: 84884171591     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01768-13     Document Type: Article
Times cited : (45)

References (34)
  • 2
    • 77952955154 scopus 로고    scopus 로고
    • Polyhydroxyalkanoates: bioplastics with a green agenda
    • Keshavarz T, Roy I. 2010. Polyhydroxyalkanoates: bioplastics with a green agenda. Curr. Opin. Microbiol. 13:321-326.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 321-326
    • Keshavarz, T.1    Roy, I.2
  • 4
    • 0024248526 scopus 로고
    • Cloning of the Alcaligenes eutrophus genes for synthesis of poly-β-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli
    • Schubert P, Steinbüchel A, Schlegel HG. 1988. Cloning of the Alcaligenes eutrophus genes for synthesis of poly-β-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli. J. Bacteriol. 170:5837-5847.
    • (1988) J. Bacteriol. , vol.170 , pp. 5837-5847
    • Schubert, P.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 6
    • 0034157704 scopus 로고    scopus 로고
    • Biosynthesis and properties of poly(3-hydroxybutyrate-co-3-hydroxyalkanoates) by recombinant strains of Pseudomonas sp. 61-3
    • Matsusaki H, Abe H, Doi Y. 2000. Biosynthesis and properties of poly(3-hydroxybutyrate-co-3-hydroxyalkanoates) by recombinant strains of Pseudomonas sp. 61-3. Biomacromolecules 1:17-22.
    • (2000) Biomacromolecule , vol.1 , pp. 17-22
    • Matsusaki, H.1    Abe, H.2    Doi, Y.3
  • 7
    • 0033004435 scopus 로고    scopus 로고
    • Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis
    • Kichise T, Fukui T, Yoshida Y, Doi Y. 1999. Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis. Int. J. Biol. Macromol. 25:69-77.
    • (1999) Int. J. Biol. Macromol. , vol.25 , pp. 69-77
    • Kichise, T.1    Fukui, T.2    Yoshida, Y.3    Doi, Y.4
  • 8
    • 0034135552 scopus 로고    scopus 로고
    • Metabolic engineering of Alcaligenes eutrophus through the transformation of cloned phbCAB genes for the investigation of the regulatory mechanism of polyhydroxyalkanoate biosynthesis
    • Jung Y, Park J, Lee Y. 2000. Metabolic engineering of Alcaligenes eutrophus through the transformation of cloned phbCAB genes for the investigation of the regulatory mechanism of polyhydroxyalkanoate biosynthesis. Enzyme Microb. Technol. 26:201-208.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 201-208
    • Jung, Y.1    Park, J.2    Lee, Y.3
  • 9
    • 38149112546 scopus 로고    scopus 로고
    • Improvement of poly(3-hydroxybutyrate) [P(3HB)] production in Corynebacterium glutamicum by codon optimization, point mutation and gene dosage of P(3HB) biosynthetic genes
    • Jo SJ, Matsumoto K, Leong CR, Ooi T, Taguchi S. 2007. Improvement of poly(3-hydroxybutyrate) [P(3HB)] production in Corynebacterium glutamicum by codon optimization, point mutation and gene dosage of P(3HB) biosynthetic genes. J. Biosci. Bioeng. 104:457-463.
    • (2007) J. Biosci. Bioeng. , vol.104 , pp. 457-463
    • Jo, S.J.1    Matsumoto, K.2    Leong, C.R.3    Ooi, T.4    Taguchi, S.5
  • 10
    • 79953309262 scopus 로고    scopus 로고
    • Improved polyhydroxybutyrate (PHB) production in transgenic tobacco by enhancing translation efficiency of bacterial PHB biosynthetic genes
    • Matsumoto K, Morimoto K, Gohda A, Shimada H, Taguchi S. 2011. Improved polyhydroxybutyrate (PHB) production in transgenic tobacco by enhancing translation efficiency of bacterial PHB biosynthetic genes. J. Biosci. Bioeng. 111:485-488.
    • (2011) J. Biosci. Bioeng. , vol.111 , pp. 485-488
    • Matsumoto, K.1    Morimoto, K.2    Gohda, A.3    Shimada, H.4    Taguchi, S.5
  • 11
    • 4544344466 scopus 로고    scopus 로고
    • Evolution of polyhydroxyalkanoate (PHA) production system by enzyme evolution: Successful case studies of directed evolution
    • Taguchi S, Doi Y. 2004. Evolution of polyhydroxyalkanoate (PHA) production system by "enzyme evolution": successful case studies of directed evolution. Macromol. Biosci. 4:146-156.
    • (2004) Macromol. Biosci , vol.4 , pp. 146-156
    • Taguchi, S.1    Doi, Y.2
  • 12
    • 33845801389 scopus 로고    scopus 로고
    • PHA synthase engineering toward superbiocatalysts for custom-made biopolymers
    • Nomura CT, Taguchi S. 2007. PHA synthase engineering toward superbiocatalysts for custom-made biopolymers. Appl. Microbiol. Biotechnol. 73:969-979.
    • (2007) Appl. Microbiol. Biotechnol. , vol.73 , pp. 969-979
    • Nomura, C.T.1    Taguchi, S.2
  • 13
    • 76649093906 scopus 로고    scopus 로고
    • Enzymatic and whole-cell synthesis of lactate-containing polyesters: toward the complete biological production of polylactate
    • Matsumoto K, Taguchi S. 2010. Enzymatic and whole-cell synthesis of lactate-containing polyesters: toward the complete biological production of polylactate. Appl. Microbiol. Biotechnol. 85:921-932.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 921-932
    • Matsumoto, K.1    Taguchi, S.2
  • 15
    • 0035917520 scopus 로고    scopus 로고
    • Analysis of mutational effects of a polyhydroxybutyrate (PHB) polymerase on bacterial PHB accumulation using an in vivo assay system
    • Taguchi S, Maehara A, Takase K, Nakahara M, Nakamura H, Doi Y. 2001. Analysis of mutational effects of a polyhydroxybutyrate (PHB) polymerase on bacterial PHB accumulation using an in vivo assay system. FEMS Microbiol. Lett. 198:65-71.
    • (2001) FEMS Microbiol. Lett. , vol.198 , pp. 65-71
    • Taguchi, S.1    Maehara, A.2    Takase, K.3    Nakahara, M.4    Nakamura, H.5    Doi, Y.6
  • 16
    • 0036244738 scopus 로고    scopus 로고
    • Enhanced accumulation and changed monomer composition in polyhydroxyalkanoate (PHA) copolyester by in vitro evolution of Aeromonas caviae PHA synthase
    • Kichise T, Taguchi S, Doi Y. 2002. Enhanced accumulation and changed monomer composition in polyhydroxyalkanoate (PHA) copolyester by in vitro evolution of Aeromonas caviae PHA synthase. Appl. Environ. Microbiol. 68:2411-2419.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2411-2419
    • Kichise, T.1    Taguchi, S.2    Doi, Y.3
  • 17
    • 0036293344 scopus 로고    scopus 로고
    • In vitro evolution of a polyhydroxybutyrate synthase by intragenic suppressiontype mutagenesis
    • Taguchi S, Nakamura H, Hiraishi T, Yamato I, Doi Y. 2002. In vitro evolution of a polyhydroxybutyrate synthase by intragenic suppressiontype mutagenesis. J. Biochem. 131:801-806.
    • (2002) J. Biochem. , vol.131 , pp. 801-806
    • Taguchi, S.1    Nakamura, H.2    Hiraishi, T.3    Yamato, I.4    Doi, Y.5
  • 18
    • 77954919291 scopus 로고    scopus 로고
    • Unprecedented acetoacetyl-coenzyme A synthesizing enzyme of the thiolase superfamily involved in the mevalonate pathway
    • Okamura E, Tomita T, Sawa R, Nishiyama M, Kuzuyama T. 2010. Unprecedented acetoacetyl-coenzyme A synthesizing enzyme of the thiolase superfamily involved in the mevalonate pathway. Proc. Natl. Acad. Sci. U. S. A. 107:11265-11270.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11265-11270
    • Okamura, E.1    Tomita, T.2    Sawa, R.3    Nishiyama, M.4    Kuzuyama, T.5
  • 19
    • 79952165865 scopus 로고    scopus 로고
    • A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase
    • Matsumoto K, Yamada M, Leong CR, Jo SJ, Kuzuyama T, Taguchi S. 2011. A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase. Biosci. Biotechnol. Biochem. 75: 364-366.
    • (2011) Biosci. Biotechnol. Biochem. , vol.75 , pp. 364-366
    • Matsumoto, K.1    Yamada, M.2    Leong, C.R.3    Jo, S.J.4    Kuzuyama, T.5    Taguchi, S.6
  • 20
    • 0037284491 scopus 로고    scopus 로고
    • Enhanced synthesis of poly(3-hydroxybutyrate) in recombinant Escherichia coli by means of error-prone PCR mutagenesis, saturation mutagenesis, and in vitro recombination of the type II polyhydroxyalkanoate synthase gene
    • Takase K, Taguchi S, Doi Y. 2003. Enhanced synthesis of poly(3-hydroxybutyrate) in recombinant Escherichia coli by means of error-prone PCR mutagenesis, saturation mutagenesis, and in vitro recombination of the type II polyhydroxyalkanoate synthase gene. J. Biochem. 133:139-145.
    • (2003) J. Biochem. , vol.133 , pp. 139-145
    • Takase, K.1    Taguchi, S.2    Doi, Y.3
  • 21
    • 33749589779 scopus 로고    scopus 로고
    • Production system for biodegradable polyester polyhydroxybutyrate by Corynebacterium glutamicum
    • Jo SJ, Maeda M, Ooi T, Taguchi S. 2006. Production system for biodegradable polyester polyhydroxybutyrate by Corynebacterium glutamicum. J. Biosci. Bioeng. 102:233-236.
    • (2006) J. Biosci. Bioeng. , vol.102 , pp. 233-236
    • Jo, S.J.1    Maeda, M.2    Ooi, T.3    Taguchi, S.4
  • 22
    • 1642566535 scopus 로고    scopus 로고
    • Alteration of substrate chain-length specificity of type II synthase for polyhydroxyalkanoate biosynthesis by in vitro evolution: in vivo and in vitro enzyme assays
    • Takase K, Matsumoto K, Taguchi S, Doi Y. 2004. Alteration of substrate chain-length specificity of type II synthase for polyhydroxyalkanoate biosynthesis by in vitro evolution: in vivo and in vitro enzyme assays. Biomacromolecules 5:480-485.
    • (2004) Biomacromolecule , vol.5 , pp. 480-485
    • Takase, K.1    Matsumoto, K.2    Taguchi, S.3    Doi, Y.4
  • 23
    • 0037229834 scopus 로고    scopus 로고
    • Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus
    • Kikuchi Y, Date M, Yokoyama K, Umezawa Y, Matsui H. 2003. Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus. Appl. Environ. Microbiol. 69:358-366.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 358-366
    • Kikuchi, Y.1    Date, M.2    Yokoyama, K.3    Umezawa, Y.4    Matsui, H.5
  • 24
    • 67649449212 scopus 로고    scopus 로고
    • Kinetic analysis of engineered polyhydroxyalkanoate synthases with broad substrate specificity
    • Matsumoto K, Shozui F, Satoh Y, Tajima K, Munekata M, Taguchi S. 2009. Kinetic analysis of engineered polyhydroxyalkanoate synthases with broad substrate specificity. Polym. J. 41:237-240.
    • (2009) Polym. J. , vol.41 , pp. 237-240
    • Matsumoto, K.1    Shozui, F.2    Satoh, Y.3    Tajima, K.4    Munekata, M.5    Taguchi, S.6
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A, Teplyako A. 1997. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyako, A.2
  • 32
    • 1542602992 scopus 로고    scopus 로고
    • Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG
    • Price AC, Zhang YM, Rock CO, White SW. 2004. Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG. Structure 12:417-428.
    • (2004) Structure , vol.12 , pp. 417-428
    • Price, A.C.1    Zhang, Y.M.2    Rock, C.O.3    White, S.W.4
  • 33
    • 0002473164 scopus 로고
    • The role of NADH-and NADPH-linked acetoacetyl-CoA reductases in the poly-3-hydroxybutyrate synthesizing organism Alcaligenes eutrophus
    • Haywood GW, Anderson AJ, Chu L, Dawes EA. 1988. The role of NADH-and NADPH-linked acetoacetyl-CoA reductases in the poly-3-hydroxybutyrate synthesizing organism Alcaligenes eutrophus. FEMS Microbiol. Lett. 52:259-264.
    • (1988) FEMS Microbiol. Lett. , vol.52 , pp. 259-264
    • Haywood, G.W.1    Anderson, A.J.2    Chu, L.3    Dawes, E.A.4
  • 34
    • 77957836517 scopus 로고    scopus 로고
    • Roles of multiple acetoacetyl coenzyme A reductases in polyhydroxybutyrate biosynthesis in Ralstonia eutropha H16
    • Budde CF, Mahan AE, Lu JN, Rha C, Sinskey AJ. 2010. Roles of multiple acetoacetyl coenzyme A reductases in polyhydroxybutyrate biosynthesis in Ralstonia eutropha H16. J. Bacteriol. 192:5319-532.8
    • (2010) J. Bacteriol. , vol.192 , pp. 5319-5328
    • Budde, C.F.1    Mahan, A.E.2    Lu, J.N.3    Rha, C.4    Sinskey, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.