| Literature DB >> 5642619 |
Abstract
1. Extracts from Moraxella lwoffi oxidize propionate, but at a low rate when compared with whole cells. 2. This oxidative activity requires the formation of propionyl-CoA. 3. Enzymes catalysing the formation of propionyl phosphate and propionyl-CoA are present. The presence of a propionyl-CoA hydrolase is considered to be an artifact, but partly responsible for the low rates of oxidation. 4. Enzymes catalysing the reduction of NAD(+) and the formation of pyruvate with propionyl-CoA as substrate are also present. 5. That the only pathway for the metabolism of propionate in extracts is a direct one to acetate via pyruvate was confirmed by the use of (14)C-labelled materials. 6. A possible sequence of enzyme-catalysed reactions that will account for the experimental observations is described.Entities:
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Year: 1968 PMID: 5642619 PMCID: PMC1198605 DOI: 10.1042/bj1070019
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857