Mutational analysis of 4-coumarate:CoA ligase identifies functionally important amino acids and verifies its close relationship to other adenylate-forming enzymes

FEBS Letters

Volumn 467, Issue 1, 2000, Pages 117-122

  Stuible, Hans Peter ^a   Büttner, Daniela ^a   Ehlting, Jürgen ^a   Hahlbrock, Klaus ^a   Kombrink, Erich ^a  

^a MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

Author keywords

Arabidopsis thaliana; Fatty acyl CoA synthetase; Luciferase; Peptide synthetase; Phenylpropanoid metabolism

Indexed keywords

LIGASE; LONG CHAIN FATTY ACID COENZYME A LIGASE; PARA COUMARIC ACID; PEPTIDE SYNTHASE;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARTICLE; ENZYME ACTIVITY; ENZYME PURIFICATION; IN VITRO STUDY; MUTATION; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACIDS; ARABIDOPSIS; BINDING SITES; CAFFEIC ACIDS; CATALYSIS; COENZYME A LIGASES; CONSERVED SEQUENCE; CYSTEINE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NUCLEOTIDES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; THERMODYNAMICS;

EID: 17544396621     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(00)01133-9     Document Type: Article

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