Regulation of biosynthesis of secondary metabolites. XVII. Purification and properties of malate dehydrogenase (decarboxylating) in Streptomyces aureofaciens
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
240762
DOI
10.1007/bf02876770
Knihovny.cz E-zdroje
- MeSH
- chemická frakcionace MeSH
- hořčík farmakologie MeSH
- koncentrace vodíkových iontů MeSH
- malátdehydrogenasa * izolace a purifikace metabolismus MeSH
- maláty metabolismus MeSH
- mangan farmakologie MeSH
- pyruváty biosyntéza MeSH
- síran amonný MeSH
- Streptomyces aureofaciens enzymologie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- hořčík MeSH
- malátdehydrogenasa * MeSH
- maláty MeSH
- mangan MeSH
- pyruváty MeSH
- síran amonný 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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