Kinetics of the inhibition of hog kidney D-amino acid oxidase by short-, medium- and long-chain fatty acids |
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Authors: | P Brachet S Carreira A Puigserver |
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Institution: | Centre de Biochimie et de Biologie Moléculaire du CNRS, Marseille, France. |
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Abstract: | Various fatty acids were studied in vitro as inhibitors of pure hog kidney D-amino acid oxidase by means of a spectrophotometric peroxidase-coupling method using D-methionine as a substrate. All the fatty acids tested behaved as substrate-competitive inhibitors of the enzyme. The affinity of the saturated aliphatic acids for D-amino acid oxidase decreased from pentanoate (5:0; Ki = 220 microM) to laurate (12:0; Ki = 675 microM), then rose to a maximum with stearate (18:0; Ki = 36 microM), suggesting the presence of a site in the active center of the enzyme that accepts long-chain fatty acid alkyl groups. Unsaturation did not further increase the affinity of the fatty acid for this binding site. |
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