Citation
Tk. Seow et al., Purification and some characteristics of a monomeric alanine racemase froman extreme thermophile, Thermus thermophilus, J BIOSCI BI, 90(3), 2000, pp. 344-346
Citations number
17
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
13891723
→ ACNP
Volume
90
Issue
3
Year of publication
2000
Pages
344 - 346
Database
ISI
SICI code
1389-1723(200009)90:3<344:PASCOA>2.0.ZU;2-9
Abstract
We purified to homogeneity an alanine racemase (EC 5.1.1.1) from Thermus th
ermophilus 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 incubati
on at 80 degreesC for 30 min.