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J Biosci Bioeng. 2000;90(3):344-6.

Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus.

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  • 1Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University, 1-1-1 Tsushima-Naka, Okayama-shi, Okayama 700-8530, Japan.


We purified to homogeneity an alanine racemase (EC from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75 degrees C, and remained active after incubation at 80 degrees C for 30 min.

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