Detail of "3130-72-1"

Reference

Acyl specificity in triglyceride synthesis by lactating rat mammary gland

Acyl specificity in triglyceride synthesis by lactating rat mammary gland. Lin, Chu Yuan; Smith, Stuart; Abraham, S. (Bruce Lyon Mem. Res. Lab., Child. Hosp. Med. Cent. North. California, Oakland, Calif., USA). J. Lipid Res., 17(6), 647-56 (English) 1976. CODEN: JLPRAW. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 13, 7 The specificity of the acyl-CoA:diglyceride acyltransferase reaction in lactating rat mammary gland was studied to provide an explanation at the enzyme level for the nonrandom distribution of fatty acids in milk fat triglycerides. Acyl-CoA:diglyceride acyltransferase activity was measured using various diglyceride and radioactive acyl-CoA substrates; products were identified as triglycerides by thin-layer and gas-liq. 1069-82-5 and 3130-72-1 which are cas registry numbers of chemicals are mentioned. chromatog. Most of the enzyme activity was located in the microsomal fraction and showed a broad specificity for the acyl donors tested (C10, C12, C14, C16, C18, and C CoA esters). The acyltransferase activity was highly specific for sn-1,2-diglyceride enantiomers; rac-1,3- and sn-2,3-diglycerides were relatively inactive. The acyl-CoA specificity was not affected by the type of 1,2-diglyceride acceptor offered, although dilaurin was the best acceptor and sn-1,2-dilaurin > sn-1,2-dimyristin > sn-1,2-dipalmitin > sn-1,2-distearin. Thus, the predominant localization of long chain fatty acids in the 1 and 2 positions, and of shorter chain fatty acids in the 3 position, of the glycerol backbone results at least in part from the specificities of the mammary gland acyltransferases. .

High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand

All Rights Reserved. High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand. Taskinen, Jukka P.; van Aalten, Daan M.In this study，3130-72-1 is also used.; Knudsen, Jens; Wierenga, Rik K. (Biocenter Oulu and Department of Biochemistry, University of Oulu FIN-90014, Finland). Proteins: Structure, Function, and Bioinformatics, 66(1), 229-238 (English) 2007 Wiley-Liss, Inc. CODEN: PSFBAF. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 75 The acyl-CoA binding protein (ACBP) is essential for the fatty acid metab., membrane structure, membrane fusion, and ceramide synthesis. Here high resoln. crystal structures of human cytosolic liver ACBP, unliganded and liganded with a physiol. ligand, myristoyl-CoA are described. The binding of the acyl-CoA mol. induces only few structural differences near the binding pocket. The crystal form of the liganded ACBP, which has two ACBP mols. in the asym. unit, shows that in human ACBP the same acyl-CoA binding pocket is present as previously described for the bovine and Plasmodium falciparum ACBP and the mode of binding of the 3'-phosphate-AMP moiety is conserved. Unexpectedly, in one of the acyl-CoA binding pockets the acyl moiety is bound in a reversed mode as compared with the bovine and P. falciparum structures. In this binding mode, the myristoyl-CoA mol. is fully ordered and bound across the two ACBP mols. of the crystallog. asym. unit: the 3'-phosphate-AMP moiety is bound in the binding pocket of one ACBP mol. and the acyl chain is bound in the pocket of the other ACBP mol. The remaining binding pocket cavities of these two ACBP mols. are filled by other ligand fragments. This novel binding mode shows that the acyl moiety can flip out of its classical binding pocket and bind elsewhere, suggesting a mechanism for the acyl-CoA transfer between ACBP and the active site of a target enzyme. This mechanism is of possible relevance for the in vivo function of ACBP. .