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Regulation of biosynthesis of secondary metabolites. XVII. Purification and properties of malate dehydrogenase (decarboxylating) in Streptomyces aureofaciens.

Authors
  • Jechová, V
  • Hostálek, Z
  • Vanĕk, Z
Type
Published Article
Journal
Folia microbiologica
Publication Date
Jan 01, 1975
Volume
20
Issue
2
Pages
137–141
Identifiers
PMID: 240762
Source
Medline
License
Unknown

Abstract

The process of isolation and purification of malate dehydrogenase (decarboxylating) (EC 1.1.1.40) from the mycelium of the actinomycete Streptomyces aureofaciens has been worked out. The enzyme was purified 35 fold. The kinetic characters of the purified enzyme are very similar to the figures for malate dehydrogenase (decarboxylating) from other sources. Km for L-malate = 2.1 X 10(-3)M, Km for NADP = 4.6 X 10(-5)M (at pH 7.4). The reaction requires metal divalent ions, Mn2+ being more effective than Mg2+. The enzyme reaches its maximal activity at pH 8.75.

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