1.1.1.283: methylglyoxal reductase (NADPH)

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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

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.283 methylglyoxal reductase (NADPH)

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Results	in table
10	Activating Compound
316	AA Sequence
1	Application
1	CAS Registry Number
13	Cloned(Commentary)
30	Cofactor
4	Crystallization (Commentary)
112	General Information
28	Inhibitors
2	kcat/KM [mM/s]
29	KM Value [mM]
27	Localization
1	Metals/Ions
8	Molecular Weight [Da]
39	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
59	Organism
7	Pathway
6	PDB ID
5	pH Optimum
1	pH Stability
1	Posttranslational Modification
4	Protein Variants
5	Purification (Commentary)
5	Reaction
51	Reference
1	Source Tissue
39	Specific Activity [micromol/min/mg]
2	Storage Stability
103	Substrates and Products (Substrate)
5	Subunits
128	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
3	Temperature Stability [°C]
17	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.283 - methylglyoxal reductase (NADPH)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified recombinant His-tagged enzyme Gre2 in apo-form and NADPH-complexed form, hanging drop vapor diffusion method, 24 mg/ml protein with or without 2 mM NADPH, with reservoir solution including 30% v/v glycerol, method, optimized, X-ray diffraction structure determination and analysis at resolutions of 2.8 and 3.02 A, respectively

Candida albicans

A0A1D8PHQ6

760931

crystal structures in an apo-form at 2.00 A and NADPH-complexed form at 2.40 A resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate

Saccharomyces cerevisiae

Q12068

737753

in complex with NADP, to 3.2 A resolution. Monoclinic space group P21, two Gre2 protomers per asymmetric unit

Saccharomyces cerevisiae

Q12068

710768

purified recombinant enzyme in apoform and in a complex with NADPH, X-ray diffraction structure determination and analysis at 2.0 A and 2.4 A, respectively

Saccharomyces cerevisiae

Q12068

741962