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

T K Seow; K Inagaki; T Nakamura; R Maeda; T Tamura; H Tanaka

doi:10.1016/s1389-1723(00)80094-8

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

J Biosci Bioeng. 2000;90(3):344-6. doi: 10.1016/s1389-1723(00)80094-8.

Authors

T K Seow¹, K Inagaki, T Nakamura, R Maeda, T Tamura, H Tanaka

Affiliation

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

PMID: 16232869
DOI: 10.1016/s1389-1723(00)80094-8

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.