1.1.1.283: methylglyoxal reductase (NADPH)
This is an abbreviated version!
For detailed information about methylglyoxal reductase (NADPH), go to the full flat file.
Reaction
Synonyms
AKR, aldo-keto reductase, AlrA, CaGre2, CANTEDRAFT_112488, D-lactaldehyde dehydrogenase, EC 1.1.1.78, Gre2, GRE2 gene product, GRE2/YOL151W, Gre2p, GRE3, GRP2, Lbuc_0522, MeGR, Mer, methylglyoxal reductase, methylglyoxal reductase (NADPH dependent), methylglyoxal/isovaleraldehyde reductase, MG reductase, MG-specific aldolase reductase, MGR, More, NADPH-dependent methylglyoxal reductase, NADPH-linked aldolase reductase, PAS_chr3_0744, SakR1, YGL039w1, YGL039w2, YOL151W, YOL151w gene product
ECTree
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Cofactor
Cofactor on EC 1.1.1.283 - methylglyoxal reductase (NADPH)
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NADPH
preferred cofactor, comparisons with NAD(P)H binding sites from other species, overview
additional information
Gre2 uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde. The cofactor-binding domain of CaGre2 adopts a typical Rossmann-fold motif, which is a beta-sheet composed of seven parallel beta-strands (beta1-7 with strand topology 3-2-1-4-5-6-7) that form the hydrophobic core of the domain surrounded by nine alpha-helices (alpha1-5, alpha7-8, alpha10, and alpha13) on both sides of the beta-sheet. Additionally, the conserved dinucleotide-binding motif (G11A12T13G14F15I16A17), which is responsible for the binding of NADPH, is exhibited as a loop followed by beta1 and a partial helix of alpha1. The C-terminal substrate-binding domain is formed by five helices (alpha6, alpha9, alpha11-12, and alpha14) and three twisted beta-strands (beta1', beta2', beta3'), with lengths ranging from 5 to 16 and from 3 to 6 residues, respectively
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