Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase

Biochemistry

Volumn 39, Issue 14, 2000, Pages 3927-3936

  Jia, Yong ^a   Kappock, T Joseph ^a   Frick, Tobias ^a   Sinskey, Anthony J ^a   Stubbe, JoAnne ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACID SYNTHASE; HISTIDINE; POLY(3 HYDROXYBUTYRIC ACID); SYNTHETASE; TRIACYLGLYCEROL LIPASE;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CHROMATIUM VINOSUM; ENZYME ACTIVE SITE; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ACYLTRANSFERASES; AMINO ACID SEQUENCE; CHROMATIUM; LIPASE; MECHANICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

ALLOCHROMATIUM VINOSUM; BACTERIA (MICROORGANISMS); CHROMATIUM; PROKARYOTA;

EID: 0034636122     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9928086     Document Type: Article

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