The aldo-keto reductase family [1,2] groups together a number of structurally
and functionally related NADPH-dependent oxidoreductases as well as some other
proteins. The proteins known to belong to this family are:
Chlordecone reductase (EC 1.1.1.225) which reduces the pesticide
chlordecone (kepone) to the corresponding alcohol.
2,5-diketo-D-gluconic acid reductase (EC 1.1.1.274) which catalyzes the
reduction of 2,5-diketogluconic acid to 2-keto-L-gulonic acid, a key
intermediate in the production of ascorbic acid.
NAD(P)H-dependent xylose reductase (EC 1.1.1.-) from the yeast Pichia
stipitis. This enzyme reduces xylose into xylit.
3-oxo-5-β-steroid 4-dehydrogenase (EC 1.3.99.6) which catalyzes the
reduction of delta(4)-3-oxosteroids.
A soybean reductase, which co-acts with chalcone synthase in the formation
of 4,2',4'-trihydroxychalcone.
Frog eye lens rho crystallin.
Yeast GCY protein, whose function is not known.
Leishmania major P110/11E protein. P110/11E is a developmentally regulated
protein whose abundance is markedly elevated in promastigotes compared with
amastigotes. Its exact function is not yet known.
Escherichia coli hypothetical protein yafB.
Escherichia coli hypothetical protein yghE.
Yeast hypothetical protein YBR149w.
Yeast hypothetical protein YHR104w.
Yeast hypothetical protein YJR096w.
These proteins have all about 300 amino acid residues. We derived 3 consensus
patterns specific to this family of proteins. The first one is located in the
N-terminal section of these proteins. The second pattern is located in the
central section. The third pattern, located in the C-terminal, is centered on
a lysine residue whose chemical modification, in aldose and aldehyde
reductases, affect the catalytic efficiency.
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