Purification and partial characterization of alanine dehydrogenase from Streptomyces aureofaciens |
| |
Authors: | Ivana Van?urová Ale? Van?ura Jind?ich Volc Ji?í Neu?zil Miroslav Flieger Gabriela Basa?ová Vladislav Běhal |
| |
Institution: | (1) Institute of Microbiology, Czechoslovak Academy of Sciences, Víde ská 1083, CS-142 20 Prague 4, Czechoslovakia;(2) Department of Fermentation Chemistry and Bioengineering, Prague Institute of Chemical Technology, Suchbátarova 5, CS-160 00 Prague 6, Czechoslovakia |
| |
Abstract: | Alanine dehydrogenase was purified to near homogeneity from cell-free extract of Streptomyces aureofaciens, which produces tetracycline. The molecular weight of the enzyme determined by size-exclusion high-performance liquid chromatography was 395 000. The molecular weight determined by sodium dodecyl sulfate gel electrophoresis was 48 000, indicating that the enzyme consists of eight subunits with similar molecular weight. The isoelectric point of alanine dehydrogenase is 6.7. The pH optimum is 10.0 for oxidative deamination of L-alanine and 8.5 for reductive amination of pyruvate. K
M values were 5.0 mM for L-alanine and 0.11 mM for NAD+. K
M values for reductive amination were 0.56 mM for pyruvate, 0.029 mM for NADH and 6.67 mM for NH4Cl.Abbreviation AlaDH
alanine dehydrogenase |
| |
Keywords: | Alanine dehydrogenase Streptomyces aureofaciens Nitrogen metabolism |
本文献已被 SpringerLink 等数据库收录! |
|