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 degrees C, and remained active after incubation at 80 degrees C for 30 min.
Seow
T K
TK
Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University, 1-1-1 Tsushima-Naka, Okayama-shi, Okayama 700-8530, Japan.
Inagaki
K
K
Nakamura
T
T
Maeda
R
R
Tamura
T
T
Tanaka
H
H