Localization of acyl carrier protein in Escherichia coli
نویسندگان
چکیده
منابع مشابه
Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein.
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 inhi...
متن کاملAmide exchange rates in Escherichia coli acyl carrier protein: correlation with protein structure and dynamics.
The acyl carrier protein (ACP) of Escherichia coli is a 77-amino acid, highly negatively charged three-helix protein that plays a central role in fatty acid biosynthesis. Previous NMR studies have suggested the presence of multiple conformations and marginally stable secondary structural elements. The stability of these elements is now examined by monitoring amide exchange in apo-ACP using NMR-...
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Mitochondrial cysteine desulfurase is an essential component of the machinery for iron-sulfur cluster biosynthesis. It has been known that human cysteine desulfurase that is catalytically active in vitro can be prepared by overexpressing in Escherichia coli cells two protein components of this system, the cysteine desulfurase protein NFS1 and the auxiliary protein ISD11. We report here that thi...
متن کاملIsolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli.
The acyl carrier protein (ACP) phosphodiesterase of Escherichia coli catalyzes the hydrolytic cleavage of the 4'-phosphopantetheine residue from ACP, with the generation of apo-ACP (P. R. Vagelos and A. R. Larrabee, J. Biol. Chem. 242:1776-1781, 1967). Although it has been postulated to play a role in the regulation of fatty acid synthesis, presently available evidence makes this unlikely, and ...
متن کاملPurification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli.
A multi-step procedure has been developed for the purification of [acyl-carrier-protein] acetyltransferase from Escherichia coli, which allows the production of small amounts of homogeneous enzyme. The subunit Mr was estimated to be 29,000 and the native Mr was estimated to be 61,000, suggesting a homodimeric structure. The catalytic properties of the enzyme are consistent with a Bi Bi Ping Pon...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1985
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.162.1.5-8.1985