Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate

Applied and Environmental Microbiology

Volumn 75, Issue 4, 2009, Pages 887-896

  Kotowska, Magdalena ^a   Pawlik, Krzysztof ^a   Smulczyk Krawczyszyn, Aleksandra ^a,c   Bartosz Bechowski, Hubert ^b   Kuczek, Katarzyna ^a  

^a INSTITUTE OF IMMUNOLOGY AND EXPERIMENTAL THERAPY   (Poland)

^b UNIVERSITY OF WROC AW   (Poland)

^c MEDianus sp z oo   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; EXTENSION MODULES; HYDROLASE; IN CONTROLS; POLYKETIDE SYNTHASE; POLYKETIDE SYNTHASES; STREPTOMYCES COELICOLOR A3(2); SUBSTRATE SPECIFICITIES; THIOESTERASE; THIOESTERASES; TYPE II;

HYBRID SYSTEMS; PLANTS (BOTANY); POLYMERS;

ENZYMES;

BACTERIUM; ENZYME ACTIVITY; ESTER; HYDROLYSIS; MUTATION; RADICAL;

ACETIC ACIDS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BUTYRATES; CATALYTIC DOMAIN; DNA MUTATIONAL ANALYSIS; FATTY ACID SYNTHETASE COMPLEX; HYDROLASES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYKETIDE SYNTHASES; PROPIONATES; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STREPTOMYCES COELICOLOR; SUBSTRATE SPECIFICITY; THIOLESTER HYDROLASES;

STREPTOMYCES COELICOLOR;

EID: 59949098326     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01371-08     Document Type: Article

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