Detail of "6244-92-4"

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Purification and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis

Purification and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis. Knudsen, Jens; Clark, Susan; Dils, Raymond (Inst. Biochem., Odense Univ., Odense, Den.). Biochem. J., 160(3), 683-91 (English) 1976. CODEN: BIJOAK. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 13 An acyl-thioester hydrolase (I) isolated from the cytosol of lactating-rabbit mammary gland, had a mol. wt. of .apprx.129,000 and terminated fatty acid synthesis at C8:0-C acids when incubated with fatty acid synthetase and malonyl CoA. I hydrolyzed acyl-CoA esters of C-C acids. Dodecanoyl-CoA was the best substrate for I, the sp. activities of 3 I prepns. being 305, 1130, and 2010 nmol dodecanoyl-CoA hydrolyzed/min/mg when 56.mu.In this experiment, several chemicals are used like 6244-92-4 and 37270-64-7 M substrate was used. I control of medium chain fatty acid synthesis by fatty acid synthetase is discussed. .

Purification and characterization of a long-chain acyl coenzyme A thioesterase from Rhodopseudomonas sphaeroides

Purification and characterization of a long-chain acyl coenzyme A thioesterase from Rhodopseudomonas sphaeroides. Boyce, Stephen G.; Leuking, Donald R. (Dep. Biol., Texas A and M Univ., College Station, TX 77843, USA). Biochemistry, 23(1), 141-7 (English) 1984. CODEN: BICHAW. ISSN: 0006-2960. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) A long-chain acyl-CoA thioesterase was purified >10,000-fold (with 38% yield) from photoheterotrophically grown cells of the facultative phototrophic organism, R. sphaeroides. This enzyme, designated thioesterase I (I), had a native mol. wt. of 22,400 as estd. by gel filtration and apparently consisted of 2 subunits of 12,500 daltons each as revealed by SDS-polyacrylamide gel electrophoresis. I only hydrolyzed acyl thio esters of CoA and displayed a strict specificity for acyl-CoA substrates where the acyl moiety was 3C12. Palmitoyl-CoA and stearoyl-CoA were the preferred satd. acyl-CoA substrates, whereas vaccenoyl-CoA was the preferred unsatd. substrate. Purified I had a pH optimum of 8.0, was stabilized by 25% glycerol, and was inhibited (90%) by treatment with 10 mM diisopropyl fluorophosphate. The phys. and biochem. properties of I resembled those reported for the Escherichia coli low-mol.-wt. thioesterase. It was proposed that R.Except for chemicals metioned above, 1763-10-6 and 6244-92-4 are also used. sphaeroides I participates in the cellular mechanism for the direct utilization of exogenously supplied fatty acids for membrane phospholipid biosynthesis. .