Kinetics of the inhibition of hog kidney D-amino acid oxidase by short-, medium- and long-chain fatty acids.
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.
Brachet
P
P
Centre de Biochimie et de Biologie Moléculaire du CNRS, Marseille, France.
Carreira
S
S
Puigserver
A
A
D000818:Animals; D001665:Binding Sites; D003605:D-Amino-Acid Oxidase / Q000037:antagonists & inhibitors*; D005227:Fatty Acids / Q000737:chemistry / Q000494:pharmacology*; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D013329:Structure-Activity Relationship; D013552:Swine
D005227:Fatty Acids; D003605:D-Amino-Acid Oxidase