A template search reveals mechanistic similarities and differences in β-ketoacyl synthases (KAS) and related enzymes

Proteins: Structure, Function and Genetics

Volumn 52, Issue 3, 2003, Pages 427-435

  Dawe, Jennifer H ^a   Porter, Craig T ^b   Thornton, Janet M ^a,b,c   Tabor, Alethea B ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b EUROPEAN BIOINFORMATICS INSTITUTE   (United Kingdom)

^c UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

3D templates; Active site residues; Enzyme catalysis; Fatty acid biosynthesis

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; ACETYL COENZYME A ACYLTRANSFERASE; CHALCONE SYNTHASE; CYSTEINE; HISTIDINE;

ARTICLE; BIOTRANSFORMATION; CATALYSIS; ENZYME ACTIVE SITE; ENZYME BINDING; METAL BINDING; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY;

3-OXOACYL-(ACYL-CARRIER-PROTEIN) SYNTHASE; BINDING SITES; COMPUTATIONAL BIOLOGY; CYSTEINE; DATABASES, PROTEIN; ENZYMES; HISTIDINE; ISOENZYMES; MALONYL COENZYME A; MOLECULAR STRUCTURE;

EID: 0042672952     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10421     Document Type: Article

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