Acyl-CoA

About: Acyl-CoA is a research topic. Over the lifetime, 527 publications have been published within this topic receiving 25134 citations. The topic is also known as: Acyl Coenzyme A.

Techniques for measuring the activity of carboxylic acid:CoA ligase and acyl-CoA:amino acid N-acyltransferase: the amino acid conjugation pathway.

Abstract: A wide variety of xenobiotic carboxylic acids are metabolized to their amino acid conjugates via a pathway that exists primarily in liver and kidney. This conjugation occurs in a two-step pathway catalyzed by two distinct types of enzymes, ligases and transferases. Measurements of acyl-CoA ligase activity include monitoring the rate of appearance of AMP or PPi, or the CoA adduct. N-acyltransferases catalyze formation of an amino acid conjugate from the CoA-activated intermediate, releasing CoA. This reaction is monitored by following the release of free CoA or the disappearance of the acyl-CoA adduct.

Effects of long-chain fatty-acyl esters of coenzyme A and carnitine on cell-free rat heart preparations

Abstract: The purpose of this study was to investigate the effects of fatty acyl CoA and carnitine esters on the glycolytic system of the rat heart. Using a respiring incubation mixture containing a whole-heart homogenate it was observed that oleoyl-CoA slowed down the glucose disappearance whereas lactate accumulation did not change. Experiments were also performed by means of an incubation mixture prepared with a soluble heart extract, considered to contain all glycolytic enzymes present in heart fibres. Palmitoyl-CoA or oleoyl-CoA as well as palmitoyl carnitine, added separately or together, were unable to alter the glucose disappearance and lactate accumulation in this mixture. These data suggest that long chain acyl-esters have not direct inhibitory actions on the heart glycolytic activity. However, CoA esters seem to exert indirect inhibitory effects which may be relevant to the myocardium under oxygen restriction situations.

PRODUCTION OF POLYUNSATURATED FATTY ACIDS BY COEXPRESSION OF ACYL-CoA:LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASES AND PHOSPHOLIPID:DIACYLGLYCEROL ACYLTRANSFERASES

Abstract: Acyl-CoA:lysophosphatidylcholine acyltransferase [“LPCAT”] having the ability to convert acyl-CoA+1-acyl-sn-glycero-3-phosphocholine to CoA+1,2-diacyl-sn-glycero-3-phosphocholine (EC 2.3.1.23) is disclosed herein to be over-expressed along with the over-expression of phospholipid:diacylglycerol acyltransferase [“PDAT”] having the ability to transfer a fatty acyl group from the sn-2 position of a phospholipid (e.g., phosphatidylcholine) to the sn-3 position of 1,2-diacylglycerol [E.C.2.3.1.158], thus resulting in a lysophospholipid and TAG. Co-expression of these enzymes in a recombinant microbial host cell resulted in increased production of long chain polyunsaturated fatty acids [“PUFAs”].

Synthesis and Hydrolysis of Wax Ester in Mullet

Abstract: The functions of enzymes in WE synthesis by plasma and roe and liver homogenates from the mullet, M. cephalus, were studied so as to clarify the metabolism of roe lipid in fish rich in wax esters (WE). The fish examined was 4, 130g in wet weight with a gonad index of 10.7. The roe was 17.6% lipid on a wet weight basis, and the amount of WE in the lipid was about 70%. Carbon numbers ranged from 30 to 34 and the major fatty acids were 16: 1 and 18: 1, and the major fatty alcohols, 16: 0 and 16: 1.WE syntheses from [1-14C] oleic acid and [1-14C] oleyl alcohol as well as the hydrolyses of oleyl [1-14C] oleate occurred to the greatest extent in the roe homogenate. The highest specific and greatest total reducing activity of [1-14C] oleic acid was also observed in this homogenate. WE synthesizing activity in roe was mainly associated with the 105, 000×g pellet and supernatant, in which WE formation from [1-14C] oleic acid was activated by the addition of ATP, CoA and NADPH. Plasma also possessed activity for WE synthesis from [1-14C] oleic acid, and its activity increased with cold oleyl alcohol in the reaction mixture.The enzymes directly related to WE synthesis from fatty acids in the mullet roe may be possibly acyl CoA: alcohol acyltransferase and fatty acid reductase, while those in plasma appear to be lecithin: alcohol acyltransferase instead of lecithin: cholesterol acyltransferase. The high content of WE in roe is possibly due to nutritional requirements and the buoyancy of eggs after hatching. The WE in roe may be one reason for its unique biochemical adaptation.