Journal of Bioscience and Bioengineering, Vol.90, No.3, 344-346, 2000
Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus
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 degreesC, and remained active after incubation at 80 degreesC for 30 min.