Artigo Acesso aberto Revisado por pares

Inhibition of Escherichia coli Acetyl Coenzyme A Carboxylase by Acyl-Acyl Carrier Protein

2001; American Society for Microbiology; Volume: 183; Issue: 4 Linguagem: Inglês

10.1128/jb.183.4.1499-1503.2001

ISSN

1098-5530

Autores

Mark S. Davis, John E. Cronan,

Tópico(s)

Enzyme Structure and Function

Resumo

ABSTRACT Escherichia coli acetyl coenzyme A carboxylase (ACC), the first enzyme of the fatty acid biosynthetic pathway, is inhibited by acylated derivatives of acyl carrier protein (ACP). ACP lacking an acyl moiety does not inhibit ACC. Acylated derivatives of ACP having chain lengths of 6 to 20 carbon atoms were similarly inhibitory at physiologically relevant concentrations. The observed feedback inhibition was specific to the protein moiety, as shown by the inability of the palmitoyl thioester of spinach ACP I to inhibit ACC.

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