Charcterization and physiological function of a soluble L-amino acid oxidase in Corynebacterium.

Archives of microbiology ·Vol. 102 ·No. 2 ·1975-00-00 ·Pages 151-3

Coudert M

Abstract

A general L-amino acid oxidase (L-amino acid: oxygen oxidoreductase (deaminating), EC(1.4.3.2) has been characterized in Corynebacterium. The enzyme is soluble (MW 130000-140000) and is active with most L-alpha-amino acids but not with aspartate, threonine, proline and glycine. It is subject to substrate inhibition. This amino acid oxidase is induced along with catalase by growth in the presence of amino acids as a nitrogen source and is repressed when ammonium ions are present in the medium. Its probable physiological function is to allow the utilization of amino acids as a nitrogen source.

MeSH Terms

Amino Acid Oxidoreductases/isolation & purification,physiology Aspartic Acid Catalase Corynebacterium/enzymology,growth & development Culture Media Enzyme Induction Glycine Nitrogen Proline Solubility Threonine

Chemicals

Culture Media Threonine Aspartic Acid Proline Catalase Amino Acid Oxidoreductases Nitrogen Glycine

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Coudert M

References (9)

9 references, click to expand

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Article Info

Journal

Archives of microbiology

Abbr.

Arch Microbiol

ISSN

0302-8933

DOI

10.1007/BF00428360

Published

1975-00-00

Pages

151-3

Language

English

Region

Germany

NLM ID

0410427

Subset

External Links

PubMed source DOI: 10.1007/BF00428360 View journal details

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Charcterization and physiological function of a soluble L-amino acid oxidase in Corynebacterium.

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