The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme

FEBS Journal

Volumn 275, Issue 24, 2008, Pages 6136-6148

  Meriläinen, Gitte ^a   Schmitz, Werner ^b   Wierenga, Rik K ^a   Kursula, Petri ^a  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

Active site; Calorimetry; Coenzyme A; Thiolase; X ray crystallography

Indexed keywords

ACETYL COENZYME A ACETYLTRANSFERASE; ALANINE; AMINO ACID DERIVATIVE; BACTERIAL ENZYME; CHOLESTEROL MONOOXYGENASE (SIDE CHAIN CLEAVING); COENZYME A; CYSTEINE; MUTANT PROTEIN; SULFUR; THIOESTER; THIOL GROUP;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CALORIMETRY; CATALYSIS; CONTROLLED STUDY; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; REACTION ANALYSIS; STRAIN DIFFERENCE; WILD TYPE; ZOOGLOEA;

BACTERIA (MICROORGANISMS); ZOOGLOEA RAMIGERA;

EID: 56849128429     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06737.x     Document Type: Article

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