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Literature summary extracted from

  • Inoue, Y.; Rhee, H.; Watanabe, K.; Murata, K.; Kimura, A.
    Metabolism of 2-oxoaldehyde in mold. Purification and characterization of two methylglyoxal reductases from Aspergillus niger (1988), Eur. J. Biochem., 171, 213-218.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.283 iodoacetate activation of enzyme MGR I, inhibition of enzyme MGR II Aspergillus niger
1.1.1.283 N-ethylmaleimide activation of enzyme MGR I, inhibition of enzyme MGR II Aspergillus niger
1.1.1.283 p-chloromercuribenzoate activation of enzyme MGR I, inhibition of enzyme MGR II Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.283 2-mercaptoethanol
-
 Aspergillus niger
1.1.1.283 Ca2+ enzymes MGR I (slightly), MGR II Aspergillus niger
1.1.1.283 Co2+ activates enzyme MGR I, slightly inhibits enzyme MGR II Aspergillus niger
1.1.1.283 Cu2+ enzymes MGR I and MGR II Aspergillus niger
1.1.1.283 dithiothreitol
-
 Aspergillus niger
1.1.1.283 EDTA
-
 Aspergillus niger
1.1.1.283 Glyoxal in absence of NADPH Aspergillus niger
1.1.1.283 iodoacetate activation of enzyme MGR I, inhibition of enzyme MGR II Aspergillus niger
1.1.1.283 methylglyoxal in absence of NADPH Aspergillus niger
1.1.1.283 Mg2+ enzymes MGR I and MGR II Aspergillus niger
1.1.1.283 Mn2+ enzymes MGR I, MGR II Aspergillus niger
1.1.1.283 N-ethylmaleimide activation of enzyme MGR I, inhibition of enzyme MGR II Aspergillus niger
1.1.1.283 NADP+
-
 Aspergillus niger
1.1.1.283 Ni2+ enzyme MGR I Aspergillus niger
1.1.1.283 p-chloromercuribenzoate activation of enzyme MGR I, inhibition of enzyme MGR II Aspergillus niger
1.1.1.283 Phenylglyoxal in absence of NADPH Aspergillus niger
1.1.1.283 Zn2+ enzyme MGR I Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.283 0.0068
-
 NADPH enzyme MGR II Aspergillus niger
1.1.1.283 0.054
-
 NADPH enzyme MGR I Aspergillus niger
1.1.1.283 0.7
-
 methylglyoxal
-
 Aspergillus niger
1.1.1.283 1.43
-
 methylglyoxal enzyme MGR I Aspergillus niger
1.1.1.283 4.35
-
 Phenylglyoxal enzyme MGR II Aspergillus niger
1.1.1.283 10
-
 Glyoxal enzyme MGR II Aspergillus niger
1.1.1.283 15.4
-
 methylglyoxal enzyme MGR I Aspergillus niger

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.283 Co2+ activates enzyme MGR I, slightly inhibits enzyme MGR II Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.283 36000
-
 1 * 36000, enzyme MGR I, 1 * 38000, enzyme MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, SDS-PAGE Aspergillus niger
1.1.1.283 37000
-
 enzyme MGR I, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration Aspergillus niger
1.1.1.283 38000
-
 enzyme MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.283 methylglyoxal + NADPH Aspergillus niger similar enzyme with NADPH requirement lactaldehyde + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.283 Aspergillus niger
-
 2 methylglyoxylate reductases: MGR I and MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.283 two methylglyoxylate reductases: MGR I and MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+ Aspergillus niger

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.283 (S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+ similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+ Aspergillus niger
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.283 0.83
-
 enzyme MGR I Aspergillus niger
1.1.1.283 7.77
-
 enzyme MGR II Aspergillus niger

Storage Stability

EC Number Storage Stability Organism
1.1.1.283 4°C Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.283 acetaldehyde + NADPH + H+ enzyme MGR II Aspergillus niger ethanol + NADP+
-
 ?
1.1.1.283 glyoxal + NADPH enzymes MGR I and MGR II Aspergillus niger glycolaldehyde + NADP+
-
 ?
1.1.1.283 methylglyoxal + NADPH similar enzyme with NADPH requirement Aspergillus niger lactaldehyde + NADP+
-
 ?
1.1.1.283 additional information enzyme MGR I: specific for 2-oxoaldehydes (glyoxal phenylglyoxal), enzyme MGR II: active towards 2-oxoaldehydes (glyoxal, methylglyoxal, phenylglyoxal), 4,5-dioxovalerate and some aldehydes (propionaldehyde and acetaldehyde) Aspergillus niger ?
-
 ?
1.1.1.283 phenylglyoxal + NADPH enzymes MGR I and MGR II Aspergillus niger hydroxyphenylacetaldehyde + NADP+
-
 ?
1.1.1.283 propionaldehyde + NADPH enzyme MGR II Aspergillus niger propanol + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.283 monomer 1 * 36000, enzyme MGR I, 1 * 38000, enzyme MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, SDS-PAGE Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.283 6.5
-
 enzyme MGR I Aspergillus niger
1.1.1.283 9
-
 enzyme MGR II Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.283 NADPH NADPH required Aspergillus niger