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.

Analysis of coenzyme A activated compounds in actinomycetes.

Abstract: Acyl-CoAs are crucial compounds involved in essential metabolic pathways such as the Krebs cycle and lipid, carbohydrate, and amino acid metabolisms, and they are also key signal molecules involved in the transcriptional regulation of lipid biosynthesis in many organisms. In this study, we took advantage of the high selectivity of mass spectrometry and developed an ion-pairing reverse-phase high-pressure liquid chromatography electrospray ionization high-resolution mass spectrometry (IP-RP-HPLC/ESI-HRMS) method to carry on a comprehensive analytical determination of the wide range of fatty acyl-CoAs present in actinomycetes. The advantage of using a QTOF spectrometer resides in the excellent mass accuracy over a wide dynamic range and measurements of the true isotope pattern that can be used for molecular formula elucidation of unknown analytes. As a proof of concept, we used this assay to determine the composition of the fatty acyl-CoA pools in Mycobacterium, Streptomyces, and Corynebacterium species, revealing an extraordinary difference in fatty acyl-CoA amounts and species distribution between the three genera and between the two species of mycobacteria analyzed, including the presence of different chain-length carboxy-acyl-CoAs, key substrates of mycolic acid biosynthesis. The method was also used to analyze the impact of two fatty acid synthase inhibitors on the acyl-CoA profile of Mycobacterium smegmatis, which showed some unexpected low levels of C24 acyl-CoAs in the isoniazid-treated cells. This robust, sensitive, and reliable method should be broadly applicable in the studies of the wide range of bacteria metabolisms in which acyl-CoA molecules participate.

Fatty acid synthesizing enzyme activity of cultured Mycobacterium lepraemurium.

Abstract: In comparing the specific activity of enzymes pertaining to the biosynthesis of fatty acids in crude extracts of cultivated M. lepraemurium and M. smegmatis, it was found that: 1. The activity of acetyl CoA carboxylase of the former organism was undetectable and that of de novo fatty acid synthetase was too weak to measure exactly, under the condition used, whereas both activities of the latter organism were comparable to those already reported by other authors. 2. The activity of acetyl CoA dependent acyl CoA elongation system of M. lepraemurium was relatively high and close to that of M. smegmatis. 3. The activities of acetyl CoA synthetase and acyl CoA synthetase of M. lepraemurium were moderately lower than those of M. smegmatis. The relation between this peculiar fatty acid synthesizing enzyme system of M. lepraemurium and its extremely sluggish growth is discussed.

In vitro studies of maleidride-forming enzymes

Abstract: In vitro assays of enzymes involved in the biosynthesis of maleidrides from polyketides in fungi were performed. The results show that the enzymes are closely related to primary metabolism enzymes of the citric acid cycle in terms of stereochemical preferences, but with an expanded substrate selectivity. A key citrate synthase can react both saturated and unsaturated acyl CoA substrates to give solely anti substituted citrates. This undergoes anti-dehydration to afford an unsaturated precursor which is cyclised in vitro by ketosteroid-isomerase-like enzymes to give byssochlamic acid.