D-AMINO ACID OXIDASE
1972; Elsevier BV; Linguagem: Inglês
10.1016/b978-0-08-016874-6.50052-7
Autores Tópico(s)Sulfur Compounds in Biology
ResumoPublisher Summary This chapter elaborates about d -amino acid oxidase. In oxidative deamination of amino acid the occurrence of α-imino acid as an intermediary substance had been proposed by reasonable chemical consideration. Regarding the structure of d -amino acid oxidase, it is well established that this enzyme consists of its apoenzyme and coenzyme FAD and has no other component. It is well known that substrate specificity of this enzyme is rather low; besides many d -amino acids, other substances such as l -proline and d -hydroxylic acids are also oxidized. Because carboxyl group is essential for a substrate or an inhibitor which competes with substrate, this group is considered to be a binding site of the substrate in combining with the enzyme protein. From the dissociation constants of the enzyme complexes with fatty acids determined according to spectrophotometric titration, the standard free energy change for the complex formation at 25°C was calculated.
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