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Aldo-keto reductase

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Aldo-keto reductase

Aldo/keto reductase family
1us0.
Identifiers
Symbol Aldo_ket_red
Pfam InterPro PROSITE PDOC00061
SCOP SUPERFAMILY 1ads
CDD cd06660

The aldo-keto reductase family is a family of enzymes that includes a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others.[1]

Structure

All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins.[2] The fold comprises a parallel beta-8/alpha-8-barrel, which contains a novel NADP-binding motif. The binding site is located in a large, deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. The hydrophobic nature of the pocket favours aromatic and apolar substrates over highly polar ones.[3]

Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking the coenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases.[4]

Examples

Some proteins of this family contain a potassium channel beta chain regulatory domain; these are reported to have oxidoreductase activity.[5]

References

This article incorporates text from the IPR001395

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