High catalytic activity of alanine racemase from psychrophilic Bacillus psychrosaccharolyticus at high temperatures in the presence of pyridoxal 5'-phosphate.

Abstract:

:We examined the effect of the pyridoxal 5'-phosphate (PLP) cofactor on the activity and stability of the psychrophilic alanine racemase, having a high catalytic activity at low temperature, from Bacillus psychrosaccharolyticus at high temperatures. The decrease in the enzyme activity at incubation temperatures over 40 degrees C was consistent with the decrease in the amount of bound PLP. Unfolding of the enzyme at temperatures above 40 degrees C was suppressed in the presence of PLP. In the presence of 0.125 mM PLP, the specific activity of the psychrophilic enzyme was higher than that of a thermophilic alanine racemase, having a high catalytic activity at high temperature, from Bacillus stearothermophilus even at 60 degrees C.

journal_name

FEMS Microbiol Lett

authors

Okubo Y,Yokoigawa K,Esaki N,Soda K,Misono H

doi

10.1111/j.1574-6968.2000.tb09377.x

keywords:

subject

Has Abstract

pub_date

2000-11-15 00:00:00

pages

169-73

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(00)00427-4

journal_volume

192

pub_type

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