A further characterization of alanine dehydrogenase from Streptomyces aureofaciens

Journal of Basic Microbiology
I VancurováV Bĕhal

Abstract

Homogeneous alanine dehydrogenase isolated from Streptomyces aureofaciens, a producer of tetracycline, was characterized from the point of its molecular and catalytic properties. Using analytical ultracentrifugation the molecular weight of alanine dehydrogenase was found to be 198,000. The enzyme could use as cofactors apart from NAD+ also 1,N6-etheno-NAD+, 3-acetylpyridine-NAD+, deamino-NAD+ and nicotinamide guanine dinucleotide. The enzyme activity in the direction of oxidative deamination was not affected by the addition of nonsubstrate amino acids, however, it was sensitive to inhibitors of SH-groups. Reductive amination of pyruvate was inhibited by L-alanine, L-serine and D-alanine. The inhibition by L-alanine and L-serine was uncompetitive with respect to NADH and noncompetitive with regard to pyruvate and ammonium ions.

References

Jul 1, 1988·The Biochemical Journal·I VancurováV Bĕhal
Jan 1, 1969·Biochimica Et Biophysica Acta·D P Borris, J N Aronson
Mar 1, 1980·Archives of Microbiology·Y Aharonowitz, C G Friedrich
Mar 1, 1964·Biochemistry·D A YPHANTIS
Jan 29, 1960·Biochimica Et Biophysica Acta·A PIERARD, J M WIAME

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Citations

Apr 26, 2019·Critical Reviews in Biotechnology·Ushmaben Chandrakantbhai Dave, Ravi-Kumar Kadeppagari
Dec 19, 2019·Journal of Molecular Microbiology and Biotechnology·Arie Van WierenSudipta Majumdar

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