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- W2039202414 abstract "An Escherichia coli mutant (fadB64), with a defective L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) which is unable to grow on long-chain fatty acids as the sole carbon source, was shown to possess a fatty acid oxidation complex that contains five beta-oxidation enzymes, including L-3-hydroxyacyl-CoA dehydrogenase. A comparative study of the complexes from the mutant, from its parental strain and from wild-type E. coli B demonstrated the immunological and gross structural identity of all three fatty acid oxidation complexes. A kinetic evaluation of the complexes led to the suggestion that the mutation may have affected the active site of L-3-hydroxyacyl-CoA dehydrogenase so that it is inactive with acetoacetyl-CoA as a substrate, but exhibits an increasing percentage of the parental dehydrogenase activity with increasing chain length of the substrate." @default.
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- W2039202414 date "1983-01-01" @default.
- W2039202414 modified "2023-09-26" @default.
- W2039202414 title "Multienzyme complexes of fatty acid oxidation from escherichia coli K-12 and from a mutant with a defective l-3-hydroxyacyl coenzyme a dehydrogenase" @default.
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- W2039202414 doi "https://doi.org/10.1016/0005-2760(83)90202-3" @default.
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