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Aldose reductase and ϱ‐crystallin belong to the same protein superfamily as aldehyde reductase
Author(s) -
Carper Deborah,
Nishimura Chihiro,
Shinohara Toshimichi,
Dietzchold Bernard,
Wistow Graeme,
Craft Cheryl,
Kador Peter,
Kinoshita Jin H.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80905-5
Subject(s) - aldehyde reductase , aldose reductase , aldo keto reductase , biochemistry , oxidoreductase , 7 dehydrocholesterol reductase , enzyme , reductase , crystallin , peptide sequence , biology , homology (biology) , complementary dna , amino acid , chemistry , gene
Aldose reductase (EC 1.1.1.21) has been implicated in a variety of diabetic complications. Here we present the first primary sequence data for the rat lens enzyme, obtained by amino acid and cDNA analysis. We have found structural similarities with another NADPH‐dependent oxidoreductase: human liver aldehyde reductase (EC 1.1.1.2). The identity between these two enzymes is 50%. Both enzymes share approx. 40–50% homology with ϱ‐crystallin, a major lens protein present only in the frog, Rana pipiens . We propose that aldose reductase, aldehyde reductase and ϱ‐crystallin are members of a superfamily of related proteins.

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