Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli
نویسندگان
چکیده
منابع مشابه
Isolation 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 کاملInhibition 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...
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in this thesis, at first we investigate the bounded inverse theorem on fuzzy normed linear spaces and study the set of all compact operators on these spaces. then we introduce the notions of fuzzy boundedness and investigate a new norm operators and the relationship between continuity and boundedness. and, we show that the space of all fuzzy bounded operators is complete. finally, we define...
15 صفحه اولAcyl carrier protein. XVII. Purification and properties of -hydroxyacyl acyl carrier protein dehydrase.
/3-Hydroxyacyl acyl carrier protein (ACP) dehydrase has been purified 2900-fold from extracts of Escherichia coli. The enzyme catalyzes the reversible dehydration of /3-hydroxyacyl-ACP thioesters to yield specifically tram-2-enoylACP products. It is active with frans-2-enoyl-ACP thioesters of chain lengths from 4 through 16 carbon atoms. The enzyme catalyzes the hydration of cis-5frans-2-dodeca...
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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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1990
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.172.9.5445-5449.1990