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)

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 s...

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Bibliographic Details
Published in:Biochemical journal 1994-11, Vol.304 ( Pt 1) (1), p.95-99
Main Authors: Labesse, G, Vidal-Cros, A, Chomilier, J, Gaudry, M, Mornon, J P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Molecular Sequence Data
NADH Dehydrogenase - chemistry
NADH, NADPH Oxidoreductases - chemistry
NADPH Dehydrogenase - chemistry
Protein Structure, Tertiary
Racemases and Epimerases - chemistry
Sequence Alignment
Structure-Activity Relationship
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3040095