메뉴 건너뛰기




Volumn 7, Issue 1, 2017, Pages

Structure of polyhydroxyalkanoate (PHA) synthase PhaC from Chromobacterium sp. USM2, producing biodegradable plastics

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; BIODEGRADABLE PLASTIC; POLY(3-HYDROXYALKANOIC ACID) SYNTHASE;

EID: 85023764107     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-05509-4     Document Type: Article
Times cited : (75)

References (57)
  • 1
    • 0034501647 scopus 로고    scopus 로고
    • Synthesis, structure and properties of polyhydroxyalkanoates: Biological polyesters
    • Sudesh, K., Abe, H. & Doi, Y. Synthesis, structure and properties of polyhydroxyalkanoates: biological polyesters. Prog. Polym. Sci. 25, 1503-1555 (2000).
    • (2000) Prog. Polym. Sci. , vol.25 , pp. 1503-1555
    • Sudesh, K.1    Abe, H.2    Doi, Y.3
  • 2
    • 84859038271 scopus 로고    scopus 로고
    • Plastics derived from biological sources: Present and future: A technical and environmental review
    • Chen, G. Q. & Patel, M. K. Plastics derived from biological sources: Present and future: A technical and environmental review. Chem. Rev. 112, 2082-2099 (2012).
    • (2012) Chem. Rev. , vol.112 , pp. 2082-2099
    • Chen, G.Q.1    Patel, M.K.2
  • 3
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: Natural catalysts for plastics
    • Rehm, B. H. A. Polyester synthases: natural catalysts for plastics. Biochem. J. 376, 15-33 (2003).
    • (2003) Biochem. J. , vol.376 , pp. 15-33
    • Rehm, B.H.A.1
  • 4
    • 22244459223 scopus 로고    scopus 로고
    • Nontemplate-dependent polymerization processes: Polyhydroxyalkanoate synthases as a paradigm
    • Stubbe, J. et al. Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm. Annu. Rev. Biochem. 74, 433-480 (2005).
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 433-480
    • Stubbe, J.1
  • 5
    • 84876667247 scopus 로고    scopus 로고
    • Polyhydroxyalkanoic acids from structurally-unrelated carbon sources in Escherichia coli
    • Wang, Q., Zhuang, Q., Liang, Q. & Qi, Q. Polyhydroxyalkanoic acids from structurally-unrelated carbon sources in Escherichia coli. Appl. Microbiol. Biotechnol. 97, 3301-3307 (2013).
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 3301-3307
    • Wang, Q.1    Zhuang, Q.2    Liang, Q.3    Qi, Q.4
  • 6
    • 84899660094 scopus 로고    scopus 로고
    • RNA-Seq analysis provides insights for understanding photoautotrophic polyhydroxyalkanoate production in recombinant Synechocystis Sp
    • Lau, N.-S., Foong, C. P., Kurihara, Y., Sudesh, K. & Matsui, M. RNA-Seq analysis provides insights for understanding photoautotrophic polyhydroxyalkanoate production in recombinant Synechocystis Sp. PLoS One 9, e86368 (2014).
    • (2014) PLoS One , vol.9 , pp. e86368
    • Lau, N.-S.1    Foong, C.P.2    Kurihara, Y.3    Sudesh, K.4    Matsui, M.5
  • 7
    • 84939547139 scopus 로고    scopus 로고
    • Production of novel biopolymers in plants: Recent technological advances and future prospects
    • Snell, K. D., Singh, V. & Brumbley, S. M. Production of novel biopolymers in plants: recent technological advances and future prospects. Curr. Opin. Biotechnol. 32, 68-75 (2015).
    • (2015) Curr. Opin. Biotechnol. , vol.32 , pp. 68-75
    • Snell, K.D.1    Singh, V.2    Brumbley, S.M.3
  • 8
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates
    • Anderson, J. & Dawes, E. A. Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiol. Rev. 54, 450-72 (1990).
    • (1990) Microbiol. Rev. , vol.54 , pp. 450-472
    • Anderson, J.1    Dawes, E.A.2
  • 9
    • 0035868599 scopus 로고    scopus 로고
    • Identification of the intracellular polyhydroxyalkanoate depolymerase gene of Paracoccus denitrificans and some properties of the gene product
    • Gao, D., Maehara, A., Yamane, T. & Ueda, S. Identification of the intracellular polyhydroxyalkanoate depolymerase gene of Paracoccus denitrificans and some properties of the gene product. FEMS Microbiol. Lett. 196, 159-164 (2001).
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 159-164
    • Gao, D.1    Maehara, A.2    Yamane, T.3    Ueda, S.4
  • 10
    • 0035803751 scopus 로고    scopus 로고
    • Occurrence, synthesis and medical application of bacterial polyhydroxyalkanoate
    • Zinn, M., Witholt, B. & Egli, T. Occurrence, synthesis and medical application of bacterial polyhydroxyalkanoate. Adv. Drug Deliv. Rev. 53, 5-21 (2001).
    • (2001) Adv. Drug Deliv. Rev. , vol.53 , pp. 5-21
    • Zinn, M.1    Witholt, B.2    Egli, T.3
  • 11
    • 15044366316 scopus 로고    scopus 로고
    • Short-chain-length polyhydroxyalkanoates: Synthesis in metabolically engineered Escherichia coli and medical applications
    • Park, S. J., Choi, J. & Lee, S. Y. Short-chain-length polyhydroxyalkanoates: Synthesis in metabolically engineered Escherichia coli and medical applications. J. Microbiol. Biotech. 15, 206-215 (2005).
    • (2005) J. Microbiol. Biotech. , vol.15 , pp. 206-215
    • Park, S.J.1    Choi, J.2    Lee, S.Y.3
  • 12
    • 84876134827 scopus 로고    scopus 로고
    • Wiley-VCH Verlag GmbH & Co. KGaA
    • Williams, S. F. & Martin, D. P. In Biopolymers Online Wiley-VCH Verlag GmbH & Co. KGaA, doi: 10.1002/3527600035.bpol4004 (2005).
    • (2005) Biopolymers Online
    • Williams, S.F.1    Martin, D.P.2
  • 13
    • 0024248526 scopus 로고
    • Cloning of the Alcaligenes eutrophus genes for synthesis of poly-beta-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli
    • Schubert, P., Steinbüchel, A. & Schlegel, H. G. Cloning of the Alcaligenes eutrophus genes for synthesis of poly-beta-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli. J. Bacteriol. 170, 5837-5847 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 5837-5847
    • Schubert, P.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 14
    • 0024425823 scopus 로고
    • Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC)
    • Peoples, O. P. & Sinskey, A. J. Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J. Biol. Chem. 264, 15298-15303 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 15298-15303
    • Peoples, O.P.1    Sinskey, A.J.2
  • 15
    • 84895945248 scopus 로고    scopus 로고
    • Engineering the diversity of polyesters
    • Meng, D.-C. et al. Engineering the diversity of polyesters. Curr. Opin. Biotechnol. 29, 24-33 (2014).
    • (2014) Curr. Opin. Biotechnol. , vol.29 , pp. 24-33
    • Meng, D.-C.1
  • 16
    • 16344375052 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate) granule-associated proteins: Impacts on poly(3-hydroxybutyrate) synthesis and degradation
    • Potter, M. & Steinbuchel, A. Poly(3-hydroxybutyrate) granule-associated proteins: impacts on poly(3-hydroxybutyrate) synthesis and degradation. Biomacromolecules 6, 552-560 (2005).
    • (2005) Biomacromolecules , vol.6 , pp. 552-560
    • Potter, M.1    Steinbuchel, A.2
  • 17
    • 0029634559 scopus 로고
    • Microbial synthesis and characterization of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate)
    • Doi, Y., Kitamura, S. & Abe, H. Microbial synthesis and characterization of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate). Macromolecules 28, 4822-4828 (1995).
    • (1995) Macromolecules , vol.28 , pp. 4822-4828
    • Doi, Y.1    Kitamura, S.2    Abe, H.3
  • 18
    • 4544344466 scopus 로고    scopus 로고
    • Evolution of polyhydroxyalkanoate (PHA) production system by 'enzyme evolution': Successful case studies of directed evolution
    • Taguchi, S. & Doi, Y. Evolution of polyhydroxyalkanoate (PHA) production system by 'enzyme evolution': Successful case studies of directed evolution. Macromol. Biosci. 4, 145-156 (2004).
    • (2004) Macromol. Biosci. , vol.4 , pp. 145-156
    • Taguchi, S.1    Doi, Y.2
  • 19
    • 78649444875 scopus 로고    scopus 로고
    • Cloning and expression of the PHA synthase gene from a locally isolated Chromobacterium sp. USM2
    • Bhubalan, K., Kam, Y. C., Yong, K. H. & Sudesh, K. Cloning and expression of the PHA synthase gene from a locally isolated Chromobacterium sp. USM2. Malays. J. Microbiol. 6, 81-90 (2010).
    • (2010) Malays. J. Microbiol. , vol.6 , pp. 81-90
    • Bhubalan, K.1    Kam, Y.C.2    Yong, K.H.3    Sudesh, K.4
  • 20
    • 77955308938 scopus 로고    scopus 로고
    • Improved synthesis of P(3HB-co-3HV-co-3HHx) terpolymers by mutant Cupriavidus necator using the PHA synthase gene of Chromobacterium sp. USM2 with high affinity towards 3HV
    • Bhubalan, K., Rathi, D. N., Abe, H., Iwata, T. & Sudesh, K. Improved synthesis of P(3HB-co-3HV-co-3HHx) terpolymers by mutant Cupriavidus necator using the PHA synthase gene of Chromobacterium sp. USM2 with high affinity towards 3HV. Polym. Degrad. Stab 95, 1436-1442 (2010).
    • (2010) Polym. Degrad. Stab , vol.95 , pp. 1436-1442
    • Bhubalan, K.1    Rathi, D.N.2    Abe, H.3    Iwata, T.4    Sudesh, K.5
  • 21
    • 79955573521 scopus 로고    scopus 로고
    • Characterization of the highly active polyhydroxyalkanoate synthase of Chromobacterium sp. Strain USM2
    • Bhubalan, K. et al. Characterization of the highly active polyhydroxyalkanoate synthase of Chromobacterium sp. strain USM2. Appl. Environ. Microbiol. 77, 2926-33 (2011).
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 2926-2933
    • Bhubalan, K.1
  • 22
    • 84997834600 scopus 로고    scopus 로고
    • Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator
    • Wittenborn, E. C., Jost, M., Wei, Y., Stubbe, J. & Drennan, C. L. Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. J. Biol. Chem. 291, 25264-25277 (2016).
    • (2016) J. Biol. Chem. , vol.291 , pp. 25264-25277
    • Wittenborn, E.C.1    Jost, M.2    Wei, Y.3    Stubbe, J.4    Drennan, C.L.5
  • 23
    • 85008881293 scopus 로고    scopus 로고
    • Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms
    • Kim, J., Kim, Y.-J., Choi, S. Y., Lee, S. Y. & Kim, K.-J. Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms. Biotechnol. J 12, 1600648 (2017).
    • (2017) Biotechnol. J , vol.12 , pp. 1600648
    • Kim, J.1    Kim, Y.-J.2    Choi, S.Y.3    Lee, S.Y.4    Kim, K.-J.5
  • 24
    • 0034636122 scopus 로고    scopus 로고
    • Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase
    • Jia, Y., Kappock, T. J., Frick, T., Sinskey, A. J. & Stubbe, J. Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase. Biochemistry 39, 3927-3936 (2000).
    • (2000) Biochemistry , vol.39 , pp. 3927-3936
    • Jia, Y.1    Kappock, T.J.2    Frick, T.3    Sinskey, A.J.4    Stubbe, J.5
  • 25
    • 0026714866 scopus 로고
    • Cloning and nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid)
    • Liebergesell, M. & Steinbüchel, A. Cloning and nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid). Chromatium vinosum strain D. Eur. J. Biochem. 209, 135-150 (1992).
    • (1992) Chromatium Vinosum Strain D. Eur. J. Biochem. , vol.209 , pp. 135-150
    • Liebergesell, M.1    Steinbüchel, A.2
  • 26
    • 0041328584 scopus 로고    scopus 로고
    • Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa-mediated synthesis of a new polyester: Identification of catalytic residues
    • Amara, A. & Rehm, B. H. Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa-mediated synthesis of a new polyester: identification of catalytic residues. Biochem. J. 374, 413-421 (2003).
    • (2003) Biochem. J. , vol.374 , pp. 413-421
    • Amara, A.1    Rehm, B.H.2
  • 27
    • 0033007185 scopus 로고    scopus 로고
    • Extracellular polymerization of 3-hydroxyalkanoate monomers with the polymerase of Alcaligenes eutrophus
    • Lenz, R. W., Farcet, C., Dijkstra, P. J., Goodwin, S. & Zhang, S. Extracellular polymerization of 3-hydroxyalkanoate monomers with the polymerase of Alcaligenes eutrophus. Int. J. Biol. Macromol. 25, 55-60 (1999).
    • (1999) Int. J. Biol. Macromol. , vol.25 , pp. 55-60
    • Lenz, R.W.1    Farcet, C.2    Dijkstra, P.J.3    Goodwin, S.4    Zhang, S.5
  • 28
    • 0034209253 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization of the polyhydroxybutyrate synthase from Ralstonia eutropha
    • Zhang, S., Yasuo, T., Lenz, R. W. & Goodwin, S. Kinetic and mechanistic characterization of the polyhydroxybutyrate synthase from Ralstonia eutropha. Biomacromolecules 1, 244-251 (2000).
    • (2000) Biomacromolecules , vol.1 , pp. 244-251
    • Zhang, S.1    Yasuo, T.2    Lenz, R.W.3    Goodwin, S.4
  • 29
    • 0034279007 scopus 로고    scopus 로고
    • In vitro polymerization and copolymerization of 3-hydroxypropionyl-CoA with the PHB synthase from Ralstonia eutropha
    • Song, J. J., Zhang, S., Lenz, R. W. & Goodwin, S. In vitro polymerization and copolymerization of 3-hydroxypropionyl-CoA with the PHB synthase from Ralstonia eutropha. Biomacromolecules 1, 433-439 (2000).
    • (2000) Biomacromolecules , vol.1 , pp. 433-439
    • Song, J.J.1    Zhang, S.2    Lenz, R.W.3    Goodwin, S.4
  • 30
    • 0033546322 scopus 로고    scopus 로고
    • Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest
    • Roussel, A. et al. Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J. Biol. Chem. 274, 16995-17002 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 16995-17002
    • Roussel, A.1
  • 31
    • 0037127266 scopus 로고    scopus 로고
    • Crystal structure of the open form of dog gastric lipase in complex with a phosphonate inhibitor
    • Roussel, A. et al. Crystal structure of the open form of dog gastric lipase in complex with a phosphonate inhibitor. J. Biol. Chem. 277, 2266-2274 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 2266-2274
    • Roussel, A.1
  • 32
    • 13444263508 scopus 로고    scopus 로고
    • Detection of intermediates from the polymerization reaction catalyzed by a D302A mutant of class III polyhydroxyalkanoate (PHA) synthase
    • Tian, J., Sinskey, A. J. & Stubbe, J. Detection of intermediates from the polymerization reaction catalyzed by a D302A mutant of class III polyhydroxyalkanoate (PHA) synthase. Biochemistry 44, 1495-1503 (2005).
    • (2005) Biochemistry , vol.44 , pp. 1495-1503
    • Tian, J.1    Sinskey, A.J.2    Stubbe, J.3
  • 33
    • 0027933456 scopus 로고
    • Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: Evidence for a required posttranslational modification for catalytic activity
    • Gerngross, T. U. et al. Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity. Biochemistry 33, 9311-9320 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9311-9320
    • Gerngross, T.U.1
  • 34
    • 0030059466 scopus 로고    scopus 로고
    • Polyhydroxybutyrate synthase: Evidence for covalent catalysis
    • Wodzinska, J. et al. Polyhydroxybutyrate synthase: Evidence for covalent catalysis. J. Am. Chem. Soc. 118, 6319-6320 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6319-6320
    • Wodzinska, J.1
  • 35
    • 0142059593 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate (PHA) hemeostasis: The role of PHA synthase
    • Stubbe, J. & Tian, J. Polyhydroxyalkanoate (PHA) hemeostasis: the role of PHA synthase. Nat. Prod. Rep. 20, 445-457 (2003).
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 445-457
    • Stubbe, J.1    Tian, J.2
  • 36
    • 84964203355 scopus 로고    scopus 로고
    • Chemistry with an artificial primer of polyhydroxybutyrate synthase suggests a mechanism for chain termination
    • Buckley, R. M. & Stubbe, J. Chemistry with an artificial primer of polyhydroxybutyrate synthase suggests a mechanism for chain termination. Biochemistry 54, 2117-2125 (2015).
    • (2015) Biochemistry , vol.54 , pp. 2117-2125
    • Buckley, R.M.1    Stubbe, J.2
  • 37
    • 0014340156 scopus 로고
    • Metabolism of poly-beta-hydroxybutyrate. I. Purification, composition, and properties of native poly-beta-hydroxybutyrate granules from Bacillus megaterium
    • Griebel, R., Smith, Z. & Merrick, J. M. Metabolism of poly-beta-hydroxybutyrate. I. Purification, composition, and properties of native poly-beta-hydroxybutyrate granules from Bacillus megaterium. Biochemistry 7, 3676-3681 (1968).
    • (1968) Biochemistry , vol.7 , pp. 3676-3681
    • Griebel, R.1    Smith, Z.2    Merrick, J.M.3
  • 38
    • 0038450995 scopus 로고    scopus 로고
    • PHA synthase from Chromatium vinosum: Cysteine 149 is involved in covalent catalysis
    • Müh, U., Sinskey, A. J., Kirby, D. P., Lane, W. S. & Stubbe, J. PHA synthase from Chromatium vinosum: cysteine 149 is involved in covalent catalysis. Biochemistry 38, 826-837 (1999).
    • (1999) Biochemistry , vol.38 , pp. 826-837
    • Müh, U.1    Sinskey, A.J.2    Kirby, D.P.3    Lane, W.S.4    Stubbe, J.5
  • 39
    • 0035969944 scopus 로고    scopus 로고
    • Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: Class I and III synthases share a similar catalytic mechanism
    • Jia, Y. et al. Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: Class I and III synthases share a similar catalytic mechanism. Biochemistry 40, 1011-1019 (2001).
    • (2001) Biochemistry , vol.40 , pp. 1011-1019
    • Jia, Y.1
  • 40
    • 84878531495 scopus 로고    scopus 로고
    • Characterization of site-specific mutations in a short-chain-length/medium-chain-length polyhydroxyalkanoate synthase: In vivo and in vitro studies of enzymatic activity and substrate specificity
    • Chuah, J. A. et al. Characterization of site-specific mutations in a short-chain-length/medium-chain-length polyhydroxyalkanoate synthase: In vivo and in vitro studies of enzymatic activity and substrate specificity. Appl. Environ. Microbiol. 79, 3813-3821 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3813-3821
    • Chuah, J.A.1
  • 41
    • 0037203912 scopus 로고    scopus 로고
    • Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: In vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model
    • Rehm, B. H. A., Antonio, R. V., Spiekermann, P., Amara, A. A. & Steinbüchel, A. Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: In vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model. Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol 1594, 178-190 (2002).
    • (2002) Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol , vol.1594 , pp. 178-190
    • Rehm, B.H.A.1    Antonio, R.V.2    Spiekermann, P.3    Amara, A.A.4    Steinbüchel, A.5
  • 42
    • 0036038421 scopus 로고    scopus 로고
    • In vivo evolution of the Aeromonas punctata polyhydroxyalkanoate (PHA) synthase: Isolation and characterization of modified PHA synthases with enhanced activity
    • Amara, A. A., Steinbuchel, A. & Rehm, B. H. A. In vivo evolution of the Aeromonas punctata polyhydroxyalkanoate (PHA) synthase: isolation and characterization of modified PHA synthases with enhanced activity. Appl. Microbiol. Biotechnol. 59, 477-482 (2002).
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 477-482
    • Amara, A.A.1    Steinbuchel, A.2    Rehm, B.H.A.3
  • 43
    • 23444436892 scopus 로고    scopus 로고
    • Site-directed saturation mutagenesis at residue F420 and recombination with another beneficial mutation of Ralstonia eutropha polyhydroxyalkanoate synthase
    • Normi, Y. M. et al. Site-directed saturation mutagenesis at residue F420 and recombination with another beneficial mutation of Ralstonia eutropha polyhydroxyalkanoate synthase. Biotechnol. Lett. 27, 705-712 (2005).
    • (2005) Biotechnol. Lett. , vol.27 , pp. 705-712
    • Normi, Y.M.1
  • 44
    • 0036293344 scopus 로고    scopus 로고
    • In Vitro Evolution of a Polyhydroxybutyrate Synthase by Intragenic Suppression-Type Mutagenesis
    • Taguchi, S., Nakamura, H., Hiraishi, T., Yamato, I. & Doi, Y. In Vitro Evolution of a Polyhydroxybutyrate Synthase by Intragenic Suppression-Type Mutagenesis. J. Biochem. 131, 801-806 (2002).
    • (2002) J. Biochem. , vol.131 , pp. 801-806
    • Taguchi, S.1    Nakamura, H.2    Hiraishi, T.3    Yamato, I.4    Doi, Y.5
  • 45
    • 36749034218 scopus 로고    scopus 로고
    • In situ proteolysis for protein crystallization and structure determination
    • Dong, A. et al. In situ proteolysis for protein crystallization and structure determination. Nat. Methods 4, 1019-1021 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 1019-1021
    • Dong, A.1
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymol 276, 307-326 (1997).
    • (1997) Methods in Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G. M. Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification. Acta Crystallogr. Sect. D Biol. Crystallogr. 66, 479-485 (2010).
    • (2010) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 49
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J. P. & Leslie, A. G. W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. Sect. D Biol. Crystallogr. 52, 30-42 (1996).
    • (1996) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 50
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. Sect. D Biol. Crystallogr. 62, 1002-1011 (2006).
    • (2006) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 51
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S. & Perrakis, A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-9 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 52
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. Sect. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 53
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. Sect. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 55
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 56
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. Sect. A 32, 922-923 (1976).
    • (1976) Acta Crystallogr. Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 57
    • 0018122036 scopus 로고
    • A rapid gas chromatographic method for the determination of poly-β-hydroxybutyric acid in microbial biomass
    • Braunegg, G., Sonnleitner, B. & Lafferty, R. M. A rapid gas chromatographic method for the determination of poly-β-hydroxybutyric acid in microbial biomass. Eur. J. Appl. Microbiol. Biotechnol. 6, 29-37 (1978).
    • (1978) Eur. J. Appl. Microbiol. Biotechnol. , vol.6 , pp. 29-37
    • Braunegg, G.1    Sonnleitner, B.2    Lafferty, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.