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Literature summary extracted from

  • Nguyen, G.; Kim, S.; Jin, H.; Cho, D.; Chun, H.; Kim, W.; Chang, J.
    Crystal structure of NADPH-dependent methylglyoxal reductase Gre2 from Candida albicans (2019), Crystals, 9, 471 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.283 gene GRE2, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3) Candida albicans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.283 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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.283 cytosol
-
 Candida albicans 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.283 methylglyoxal + NADH + H+ Candida albicans
-
 (S)-lactaldehyde + NAD+
-
 ?
1.1.1.283 methylglyoxal + NADH + H+ Candida albicans ATCC MYA-2876
-
 (S)-lactaldehyde + NAD+
-
 ?
1.1.1.283 methylglyoxal + NADPH + H+ Candida albicans
-
 (S)-lactaldehyde + NADP+
-
 ?
1.1.1.283 methylglyoxal + NADPH + H+ Candida albicans ATCC MYA-2876
-
 (S)-lactaldehyde + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.283 Candida albicans A0A1D8PHQ6
-
-
1.1.1.283 Candida albicans ATCC MYA-2876 A0A1D8PHQ6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.283 recombinant His-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography and preparative gel filtration Candida albicans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.283 methylglyoxal + NADH + H+
-
 Candida albicans (S)-lactaldehyde + NAD+
-
 ?
1.1.1.283 methylglyoxal + NADH + H+
-
 Candida albicans ATCC MYA-2876 (S)-lactaldehyde + NAD+
-
 ?
1.1.1.283 methylglyoxal + NADPH + H+
-
 Candida albicans (S)-lactaldehyde + NADP+
-
 ?
1.1.1.283 methylglyoxal + NADPH + H+
-
 Candida albicans ATCC MYA-2876 (S)-lactaldehyde + NADP+
-
 ?
1.1.1.283 additional information CaGre2 exhibits a stronger affinity for NADPH than NADH Candida albicans ?
-
-
1.1.1.283 additional information CaGre2 exhibits a stronger affinity for NADPH than NADH Candida albicans ATCC MYA-2876 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.1.1.283 CaGre2
-
 Candida albicans
1.1.1.283 Gre2
-
 Candida albicans
1.1.1.283 Gre2p
-
 Candida albicans
1.1.1.283 NADPH-dependent methylglyoxal reductase
-
 Candida albicans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.283 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 Candida albicans
1.1.1.283 NADH
-
 Candida albicans
1.1.1.283 NADPH preferred cofactor, comparisons with NAD(P)H binding sites from other species, overview Candida albicans

General Information

EC Number General Information Comment Organism
1.1.1.283 evolution the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. The 3D structures of SDR enzymes all display a typical Rossman fold for cofactor binding with highly similar alpha/beta patterns and a central beta-sheet. Furthermore, the key active site, a catalytic triad of Tyr, Lys, and Ser, is found in almost all SDR forms Candida albicans
1.1.1.283 additional information enzyme sequence and structure comparisons, overview Candida albicans
1.1.1.283 physiological function Gre2 is a key enzyme in the methylglyoxal detoxification pathway. It uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde Candida albicans