Regulation of biosynthesis of secondary metabolites

Autor: Zdenko Vaněk, Z. Hošťálek, V. Jechová
Rok vydání: 1975
Předmět:
Zdroj: Folia Microbiologica. 20:137-141
ISSN: 1874-9356
0015-5632
DOI: 10.1007/bf02876770
Popis: 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.
Databáze: OpenAIRE