ISOLATION AND PROPERTIES OF ACYL CARRIER PROTEIN PHOSPHODIESTERASE OF ESCHERICHIA-COLI
ISOLATION AND PROPERTIES OF ACYL CARRIER PROTEIN PHOSPHODIESTERASE OF ESCHERICHIA-COLI
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DOI：
10.1128/jb.172.9.5445-5449.1990
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发表时间：
1990-09-01
影响因子：
3.2
通讯作者：
KENNEDY, EP
中科院分区：
文献类型：
--
作者：
FISCHL, AS;KENNEDY, EP
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 its physiological function requires further investigation. We have now purified the enzyme from E. coli more than 3,000-fold and have identified it as a protein of Mr 25,000, as judged from its migration during electrophoresis in gels containing sodium dodecyl sulfate. The emzyme has remarkable thermostability, being protected against irreversible inactivation of 90.degree.C by the presence of sodium dodecyl sulfate. A partial sequence of the amino acid terminus of the enzyme is as follows: H2N-Ser-Lys-Val-Leu-Val-Leu-Lys-Ser-?-Ile-Leu-Ala-Gly-Tyr-Ser-. Other properties of the enzyme are also described.
