Disease relevance of Decanoyl-coenzyme A

• This residual activity indicates the presence of an additional decanoyl-CoA hydrolase in E. coli [1].

High impact information on Decanoyl-coenzyme A

• A purified histidine-tagged Pte1p showed high activity toward short and medium chain length acyl-CoAs, including butyryl-CoA, decanoyl-CoA and 8-methyl-nonanoyl-CoA [2].
• Lauroyl-CoA (C12) was about half as effective as palmitoyl-CoA, and decanoyl-CoA (C10) and butyl-CoA (C4) were inactive [3].
• E. coli strains having a large deletion within the genomic tesB gene grew normally but retained a low level of thioesterase activity toward decanoyl-CoA [1].
• We have now analysed the complete beta-oxidation of 5-HD-CoA using specially synthesised (and purified) substrates and enzymes, as well as isolated rat liver and heart mitochondria, and compared it with the metabolism of the physiological substrate decanoyl-CoA [4].
• Consistent with the kinetic data, 5-hydroxydecanoyl-CoA alone acted as a weak substrate in isolated mitochondria, whereas addition of 100 mum 5-HD-CoA inhibited the metabolism of decanoyl-CoA or lauryl-carnitine [4].

Biological context of Decanoyl-coenzyme A

• The partially purified membrane and the matrix enzymes showed broad substrate specificity, and the highest enzyme activities for both were observed with decanoyl-CoA [5].

Anatomical context of Decanoyl-coenzyme A

• 1. Acyl-CoA hydrolase activities, using palmitoyl-CoA and decanoyl-CoA as substrates, were highest in the proximal part and lowest in the distal part of the guinea-pig small intestine [6].
• When peroxisomes were incubated with [9,10-(3)H]palmitate and [9,10-(3)H]stearate, among medium-chain acyl-CoAs, octanoyl-CoA and decanoyl-CoA were primarily detected, respectively, suggesting the occurrence of at least 4 cycles of beta-oxidation of both fatty acids by peroxisomes [7].

Gene context of Decanoyl-coenzyme A

• We found the recombinant beta-cell K(ATP) channel (SUR1/Kir6.2) to be much less sensitive to medium-chain acyl CoAs (decanoyl CoA: 124% +/- 15% v 231% +/- 25% in SUR2A/Kir6.2), suggesting a role for the cardiac sulfonylurea receptor, SUR2A, in the molecular mechanism of activation by these compounds [8].
• These results suggest that MCAD-deficient cells readily convert decanoyl-CoA into octanoyl-CoA [9].

Analytical, diagnostic and therapeutic context of Decanoyl-coenzyme A

• The products formed from [1-14C]acetyl-CoA and decanoyl-CoA in this reconstituted system were analyzed by thin-layer chromatography and radio-gas-liquid chromatography [10].

References