1.1.1.283: methylglyoxal reductase (NADPH)

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For detailed information about methylglyoxal reductase (NADPH), go to the full flat file.

Word Map on EC 1.1.1.283

1.1.1.283

laccase

nadh-dcip

malachite

reductases

textile

kluyveromyces

violet

biosorption

lignin

wastewater

recalcitrant

uv-visible

marxianus

synthesis

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]

Subunits

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Subunits on EC 1.1.1.283 - methylglyoxal reductase (NADPH)

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homodimer

Saccharomyces cerevisiae

Q12068

enzyme 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

741962

monomer

4 entries