A common active site of polyhydroxyalkanoate synthase from Bacillus cereus YB-4 is involved in polymerization and alcoholysis reactions

Applied Microbiology and Biotechnology

Volumn 99, Issue 11, 2015, Pages 4701-4711

  Hyakutake, Manami ^a,b   Tomizawa, Satoshi ^c   Mizuno, Kouhei ^d   Hisano, Tamao ^e   Abe, Hideki ^a,b   Tsuge, Takeharu ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b RIKEN Center for Sustainable Resource Science   (Japan)

^c KUMAMOTO NATIONAL COLLEGE OF TECHNOLOGY   (Japan)

^d KITAKYUSHU NATIONAL COLLEGE OF TECHNOLOGY   (Japan)

^e RIKEN SPring 8 Center ^*  (Japan)

Author keywords

Alcoholysis; Bacillus; Catalytic residue; Class IV PHA synthase; Escherichia coli; Polyhydroxyalkanoate

Indexed keywords

AMINO ACIDS; BACILLI; BACTERIOLOGY; CHAINS; ESCHERICHIA COLI; MUTAGENESIS; POLYMERIZATION; POLYMERS;

ALCOHOLYSIS; ALCOHOLYSIS REACTIONS; CATALYTIC RESIDUE; PHA SYNTHASES; POLY-HYDROXYALKANOATE; POLYHYDROXYALKANOATE SYNTHASE; POLYHYDROXYALKANOATES; POLYMERIZATION ACTIVITY;

BACILLUS CEREUS;

ACYLTRANSFERASE; POLY(3-HYDROXYALKANOIC ACID) SYNTHASE;

AMINO ACID SUBSTITUTION; BACILLUS CEREUS; DNA MUTATIONAL ANALYSIS; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; METABOLISM; POLYMERIZATION;

ACYLTRANSFERASES; AMINO ACID SUBSTITUTION; BACILLUS CEREUS; CATALYTIC DOMAIN; DNA MUTATIONAL ANALYSIS; POLYMERIZATION;

EID: 84937641763     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6276-4     Document Type: Article

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