Regulation of biosynthesis of secondary metabolites. XVII. Purification and properties of malate dehydrogenase (decarboxylating) in Streptomyces aureofaciens
Language English Country United States Media print
Document type Journal Article
PubMed
240762
DOI
10.1007/bf02876770
Knihovny.cz E-resources
- MeSH
- Chemical Fractionation MeSH
- Magnesium pharmacology MeSH
- Hydrogen-Ion Concentration MeSH
- Malate Dehydrogenase * isolation & purification metabolism MeSH
- Malates metabolism MeSH
- Manganese pharmacology MeSH
- Pyruvates biosynthesis MeSH
- Ammonium Sulfate MeSH
- Streptomyces aureofaciens enzymology metabolism MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Magnesium MeSH
- Malate Dehydrogenase * MeSH
- Malates MeSH
- Manganese MeSH
- Pyruvates MeSH
- Ammonium Sulfate MeSH
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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