Isolation and characterization of a mitochondrial d amino acid oxidase from Neurospora crassa

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) acti...

Full description

Saved in:
Bibliographic Details
Published inCanadian journal of biochemistry Vol. 55; no. 1; pp. 66 - 74
Main Authors Rosenfeld, M.G, Leiter, E.H
Format Journal Article
LanguageEnglish
Published Canada 1977
Subjects
Cell Fractionation
D-Amino-Acid Oxidase - isolation & purification
D-Amino-Acid Oxidase - metabolism
fungi
Hydrogen-Ion Concentration
Kinetics
Mitochondria - enzymology
Neurospora - enzymology
Neurospora crassa - enzymology
Structure-Activity Relationship
Temperature
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0008-4018
DOI:10.1139/o77-012