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Enhancement of the turnover number of thermostable malate dehydrogenase by deleting hydrogen bonds around the catalytic site.

Abstract：

:In malate dehydrogenase from Thermus flavus, substitution of Ile for Thr189, which is involved in hydrogen-bond network around a loop containing catalytic His186, caused an increase in the turnover number at room temperatures. In order to examine the effect of disruption of the hydrogen bonds on the catalytic activity, residues participating in the network were replaced by others which cannot form hydrogen bond by site-directed mutagenesis. All the mutations caused increases in the turnover number at room temperatures. This result suggests that an increase in flexibility introduced around catalytic site enhanced the catalytic activity of the malate dehydrogenase.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Nishiyama M,Kinoshita M,Kudo H,Horinouchi S,Tanokura M

doi

10.1006/bbrc.1996.1261

subject

Has Abstract

pub_date

1996-08-23 00:00:00

pages

844-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91261-9

journal_volume

225

pub_type

杂志文章

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