Results 151 to 160 of about 12,733 (207)

A tailored enzyme cascade facilitates DNA-encoded library technology and gives access to a broad substrate scope

Buller R, Schaub D, Lessing A, Meyer F, Eichenberger M, von Haugwitz G, Stockinger P, Gloger A, Scheuermann J.   +8 more
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Serine carboxypeptidase-like acyltransferases

Phytochemistry, 2004
In plant secondary metabolism, an alternative pathway of ester formation is facilitated by acyltransferases accepting 1-O-beta-acetal esters (1-O-beta-glucose esters) as acyl donors instead of coenzyme A thioesters. Molecular data indicate homology of these transferases with hydrolases of the serine carboxypeptidase type defining them as serine ...
Carsten Milkowski, Dieter Strack
exaly   +3 more sources

Phospholipases and acyltransferases in macrophages

Klinische Wochenschrift, 1989
In contrast to many other cells, macrophages contain a phospholipase A2, which preferentially liberates arachidonic acid from the main phospholipids. In unstimulated macrophages this acylchain-specific phospholipase A2 is localized in the lipid-free cytosol and thus without function.
I, Flesch, T, Schonhardt, E, Ferber
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Physiological Functions of Phospholipid:Diacylglycerol Acyltransferases

Plant And Cell Physiology, 2023
Abstract Triacylglycerol (TAG) is among the most energy dense storage forms of reduced carbon in living systems. TAG metabolism plays critical roles in cellular energy balance, lipid homeostasis, cell growth and stress responses. In higher plants, microalgae and fungi, TAG is assembled by acyl-CoA-dependent and acyl-CoA-independent ...
Saroj Kumar Sah, Jilian Fan, Jantana Blanford, John Shanklin, Changcheng Xu   +4 more
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Dihydroxyacetone phosphate acyltransferase

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1997
In this article the properties, assay, distribution, subcellular localization, deficiency in congenital peroxisomal disorders, purification and physiological functions of dihydroxyacetone phosphate acyltransferase (EC 2.3.1.42) are reviewed.
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ACYL-COENZYME A:CHOLESTEROL ACYLTRANSFERASE

Annual Review of Biochemistry, 1997
Due to its presumed role in regulating cellular cholesterol homeostasis, and in various pathophysiological conditions, acyl-coenzyme A:cholesterol acyltransferase (ACAT) has attracted much attention. Cloning the ACAT gene provides the necessary tool to advance molecular studies of this enzyme.
T Y, Chang, C C, Chang, D, Cheng
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Lecithin cholesterol acyltransferase

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2000
Cholesterol transport in circulation and its removal from tissues depends on the activity of lecithin cholesterol acyltransferase (LCAT). LCAT is a soluble enzyme that converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lyso-phosphatidylcholines on the surface of high-density lipoproteins.
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Inhibitors of Acyl CoA:Cholesterol Acyltransferase

Journal of Medicinal Chemistry, 1996
Conformational restriction of previously disclosed acyclic (diphenylethyl)diphenylacetamides led to the discovery of several potent inhibitors of acyl CoA:cholesterol acyltransferase (ACAT). cis-[2-(4-Hydroxyphenyl)-1-indanyl]diphenylacetamide (4a) was the most potent ACAT inhibitor identified (IC50 = 0.04 microM in an in vitro rat hepatic microsomal ...
W, Vaccaro, C, Amore, J, Berger, R, Burrier, J, Clader, H, Davis, M, Domalski, T, Fevig, B, Salisbury, R, Sher   +9 more
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