Thermostable alanine dehydrogenase of Bacillus sp. DSM730: gene cloning, purification, and characterization

Biochimie
S NagataK Soda

Abstract

We have cloned the thermostable alanine dehydrogenase (EC 1.4.1.1) gene from a thermophile, Bacillus sp. DSM730, into Escherichia coli C600 with a vector plasmid, pBR322. The enzyme was overproduced by the transformed cells, and purified to homogeneity with a yield of 69% by heat treatment and another step. The enzyme has a molecular weight of about 250,000 and consists of 6 subunits identical in molecular weight (43,000). It is not inactivated by heat treatment at 75 degrees C for 60 min, or incubation in the pH range of 5.5-10.5 at 55 degrees C for 10 min. The enzyme ctalyzes the oxidative deamination of L-serine in addition to L-alanine. The oxo analogue of serine is as reactive as pyruvate. Thus, the enzyme differs markedly from alanine dehydrogenases so far studied.

References

Oct 1, 1979·European Journal of Biochemistry·T Ohashima, K Soda
Feb 1, 1974·Journal of Bacteriology·Y NittaY Hachisuka
Feb 15, 1983·Biochimica Et Biophysica Acta·L MureşanO Bârzu

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