D175 DISCRIMINATES BETWEEN NADH AND NADPH IN THE COENZYME BINDING-SITE OF LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS D-LACTATE DEHYDROGENASE

被引：40
作者：
BERNARD, N
JOHNSEN, K
HOLBROOK, JJ
DELCOUR, J
机构：
[1] UNIV CATHOLIQUE LOUVAIN,UNITE GENET,MOLEC GENET LAB,B-1348 LOUVAIN,BELGIUM
[2] UNIV BRISTOL,CTR MOLEC RECOGNIT,BRISTOL,AVON,ENGLAND
[3] UNIV BRISTOL,DEPT BIOCHEM,BRISTOL,AVON,ENGLAND
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 208卷 / 03期
关键词：
D O I：
10.1006/bbrc.1995.1419
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The NAD-dependent D-(-)-lactate dehydrogenase (D-LDH) from Lactobacillus delbrueckii subsp. bulgaricus (in short, L. bulgaricus) has been modified at position 175 by site-directed mutagenesis, changing a conserved aspartate residue into an alanine. The D175A mutant enzyme displays a 40-fold shift in coenzyme preference from NADH to NADPH. This demonstrates that D175 truly belongs to the amino acid consensus GXGXXGX((17))D (where X represents any residue) which is the signature of the coenzyme binding site of most NAD-dependent dehydrogenases. (C) 1995 Academic Press, Inc.
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页码：895 / 900
页数：6
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