Faculty Research 1970 - 1979

Title

Isolation and characterization of a mitochondrial D-amino acid oxidase from Neurospora crassa.

Document Type

Article

Publication Date

1977

Keywords

D-Amino-Acid-Oxidase: ip, me, Hydrogen-Ion-Concentration, Kinetics, Mitochondria: en, Neurospora: en, Neurospora-Crassa: en, Structure-Activity-Relationship, Temperature

JAX Source

Can-J-Biochem. 1977 Jan; 55(1):66-74.

Abstract

D-Amino acid oxidase (EC 1.4.3.3) activity in homogenates of Neurospora crassa strain SY7A was found to sediment with the mitochondrial fraction. Digitonin fractionation studies on purified mitochondria have indicated a matrix localization of the enzyme. Additionally, a peroxidase (EC 1.11.1.7) activity, which may remove hydrogen peroxide formed as a product of D-amino acid oxidation, was also found in the mitochondrial matrix. Partial purification (20- to 30-fold) of the mitochondrial D-amino acid oxidase was achieved. The enzyme exhibited a pH optimum between 9.0 and 9.2, temperature optimum between 20 and 30 degrees C, and a molecular weight of 118 000 +/- 6000 as determined by gel electrophoresis and 125 000 as determined by gel chromatography.

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