title: Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus.
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.
authors.affiliation: Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University, 1-1-1 Tsushima-Naka, Okayama-shi, Okayama 700-8530, Japan.
authors.forename: T K
authors.initials: TK
authors.lastname: Seow
authors.forename: K
authors.initials: K
authors.lastname: Inagaki
authors.forename: T
authors.initials: T
authors.lastname: Nakamura
authors.forename: R
authors.initials: R
authors.lastname: Maeda
authors.forename: T
authors.initials: T
authors.lastname: Tamura
authors.forename: H
authors.initials: H
authors.lastname: Tanaka