FLAVOENZYME CATALYSIS. SUBSTRATE-COMPETITIVE INHIBITION OF d-AMINO ACID OXIDASE
نویسندگان
چکیده
منابع مشابه
Flavoenzyme catalysis: substrate-competitive inhibition of D-amino acid oxidase.
In an earlier paper from this laboratory (1) there were described the characteristics of competitive inhibition resulting from the interference of certain aromatic compounds with the association of flavin adenine dinucleotide and the separated protein of n-amino acid oxidase. Included among the inhibitors were auramine, quinine, and various other quinolines and anilines. We now present our find...
متن کاملInhibition of D - Amino Acid Oxidase
In an earlier paper from this laboratory (1) there were described the characteristics of competitive inhibition resulting from the interference of certain aromatic compounds with the association of flavin adenine dinucleotide and the separated protein of n-amino acid oxidase. Included among the inhibitors were auramine, quinine, and various other quinolines and anilines. We now present our find...
متن کاملINHIBITION OF THE d-AMINO ACID OXIDASE BY BENZOIC ACID
Benzoic acid has been reported to inhibit the oxidation of succinic acid by muscle (l), the oxidation of butyric acid and crotonic acid by liver slices (2), and the oxidation of acetoacetic acid by kidney slices (3). It has also been reported to inhibit the oxygen uptake of liver and kidney slices, diaphragm, minced liver, kidney, and brain (4). In the present work it was found that benzoic aci...
متن کاملEngineering the substrate specificity of D-amino-acid oxidase.
The high resolution crystal structure of D-amino-acid oxidase (DAAO) from the yeast Rhodotorula gracilis provided us with the tool to engineer the substrate specificity of this flavo-oxidase. DAAO catalyzes the oxidative deamination of D-amino acids, with the exception of D-aspartate and D-glutamate (which are oxidized by D-aspartate oxidase, DASPO). Following sequence homology, molecular model...
متن کاملInhibition of D-amino acid oxidase by aromatic acids.
Benzoate competes with n-amino acids for n-amino acid oxidase and thus inhibits the activity of the oxidase (l-3). Monosubstituted benzoates, depending upon the substituent, have higher and lower affinities for the oxidase than has benzoate (2). Kojic acid, a Y-pyrone, likewise competitively inhibits the oxidase (4). The present report describes the inhibition of n-amino acid oxidase by certain...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1956
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65118-x