Ratio of active to inactive forms 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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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...
متن کاملMutants of Escherichia coli with temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase.
We have characterized two mutants of Escherichia coli in which fatty acid biosynthesis is adversely affected by elevated temperature. Under conditions which do not alter the activity of wild type cell-free extracts, virtually all of the malonyl coenzyme A-acyl carrier protein (ACP) transacylase and fatty acid synthetase activities present in mutant extracts are thermolabile. Malonyl transacylas...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43791-4