Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus |
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| Authors: | Seow T K Inagaki K Nakamura T Maeda R Tamura T Tanaka H |
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| Affiliation: | Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University, 1-1-1 Tsushima-Naka, Okayama-shi, Okayama 700-8530, Japan. |
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| Abstract: | We purified to homogeneity an alanine racemase (EC 5.1.1.1) 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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