STRUCTURAL COMPARISONS LEAD TO THE DEFINITION OF A NEW SUPERFAMILY OF NAD(P)(H)-ACCEPTING OXIDOREDUCTASES - THE SINGLE-DOMAIN REDUCTASES/EPIMERASES/DEHYDROGENASES (THE RED FAMILY)

被引：63

作者：

LABESSE, G

VIDALCROS, A

CHOMILIER, J

GAUDRY, M

MORNON, JP

机构：

[1] UNIV PARIS 07, CNRS, URA 09, F-75252 PARIS 05, FRANCE

[2] UNIV PARIS 06, CHIM ORGAN BIOL LAB, CNRS, URA 493, F-75252 PARIS 05, FRANCE

来源：

BIOCHEMICAL JOURNAL | 1994年 / 304卷

关键词：

D O I：

10.1042/bj3040095

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：

Using both primary- and tertiary-structure comparisons, we have established new structural similarities shared by reductases, epimerases and dehydrogenases not previously known to be related. Despite the low sequence identity (down to 10%), short consensus segments are identified. We show that the sequence, the active site and the supersecondary structure are well conserved in these proteins. New homologues (the protochlorophyllide reductases) are detected, and we define a new superfamily composed of single-domain dinucleotide-binding enzymes. Rules for the cofactor-binding specificity are deduced from our sequence alignment. The involvement of some amino acids in catalysis is discussed. Comparison with two-domain dehydrogenases allows us to distinguish two general mechanisms of divergent evolution.

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页码：95 / 99

页数：5

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