Activities | Families | Sequences | Fold types | References | Help
B6db references: notinpubmed

type Journal Article
authors Kim, S.S; Yu, Y.G.
title Molecular cloning of an eExtremely thermostable alanine racemase from Aquifex pyrophilus and enzymatic characterization of the expressed protein
journal J Biochem Mol Biol
sel selected
ui NOTinPubmed
year (2000)
volume 33
number \
pages 82-8
keywords Alanine Racemase/*thermostable
abstract A homologous gene to alanine racemase was cloned from a hyperthermophilic bacterium, Aquifex pyrophilus. The cloned gene encodes a protein of 341 amino acids, which has a significant homology to alanine racemase of Bacillus stearothermophilus, Lactobacillus brevis, and E. coli. When the gene was expressed in Escherichia coli, it produced a 40 kDa protein. The purified protein contains one mole pyridoxal 5-phosphate per one mole of protein, which is essential for catalytic activity of alanine racemase. The purified protein catalyzed racemization of L-alanine to D-alanine, or vice versa, indicating that the cloned gene encoded alanine racemase. It also showed significant racemization activity against L-serine and a-aminobutylic acid. The A. pyrophilus alanine racemase showed strong thermostability, and it maintained catalytic activity in the presence of organic solvents.
last changed 2010/06/14 10:48

B6db references