BRENDA - Enzyme Database show
show all sequences of 1.1.1.283

Metabolism of 2-oxoaldehyde in mold. Purification and characterization of two methylglyoxal reductases from Aspergillus niger

Inoue, Y.; Rhee, H.; Watanabe, K.; Murata, K.; Kimura, A.; Eur. J. Biochem. 171, 213-218 (1988)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
iodoacetate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
N-ethylmaleimide
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
p-chloromercuribenzoate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
-
Aspergillus niger
Ca2+
enzymes MGR I (slightly), MGR II
Aspergillus niger
Co2+
activates enzyme MGR I, slightly inhibits enzyme MGR II
Aspergillus niger
Cu2+
enzymes MGR I and MGR II
Aspergillus niger
dithiothreitol
-
Aspergillus niger
EDTA
-
Aspergillus niger
Glyoxal
in absence of NADPH
Aspergillus niger
iodoacetate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
methylglyoxal
in absence of NADPH
Aspergillus niger
Mg2+
enzymes MGR I and MGR II
Aspergillus niger
Mn2+
enzymes MGR I, MGR II
Aspergillus niger
N-ethylmaleimide
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
NADP+
-
Aspergillus niger
Ni2+
enzyme MGR I
Aspergillus niger
p-chloromercuribenzoate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
Phenylglyoxal
in absence of NADPH
Aspergillus niger
Zn2+
enzyme MGR I
Aspergillus niger
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0068
-
NADPH
enzyme MGR II
Aspergillus niger
0.054
-
NADPH
enzyme MGR I
Aspergillus niger
0.7
-
methylglyoxal
-
Aspergillus niger
1.43
-
methylglyoxal
enzyme MGR I
Aspergillus niger
4.35
-
Phenylglyoxal
enzyme MGR II
Aspergillus niger
10
-
Glyoxal
enzyme MGR II
Aspergillus niger
15.4
-
methylglyoxal
enzyme MGR I
Aspergillus niger
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
activates enzyme MGR I, slightly inhibits enzyme MGR II
Aspergillus niger
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
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
37000
-
enzyme MGR I, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration
Aspergillus niger
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)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methylglyoxal + NADPH
Aspergillus niger
similar enzyme with NADPH requirement
lactaldehyde + NADP+
-
Aspergillus niger
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
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)
Commentary
Organism
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
Reaction
Commentary
Organism
(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
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.83
-
enzyme MGR I
Aspergillus niger
7.77
-
enzyme MGR II
Aspergillus niger
Storage Stability
Storage Stability
Organism
4°C
Aspergillus niger
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + NADPH + H+
enzyme MGR II
207974
Aspergillus niger
ethanol + NADP+
-
207974
Aspergillus niger
?
glyoxal + NADPH
enzymes MGR I and MGR II
207974
Aspergillus niger
glycolaldehyde + NADP+
-
207974
Aspergillus niger
?
methylglyoxal + NADPH
similar enzyme with NADPH requirement
207974
Aspergillus niger
lactaldehyde + NADP+
-
207974
Aspergillus niger
?
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)
207974
Aspergillus niger
?
-
-
-
-
phenylglyoxal + NADPH
enzymes MGR I and MGR II
207974
Aspergillus niger
hydroxyphenylacetaldehyde + NADP+
-
207974
Aspergillus niger
?
propionaldehyde + NADPH
enzyme MGR II
207974
Aspergillus niger
propanol + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
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
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
enzyme MGR I
Aspergillus niger
9
-
enzyme MGR II
Aspergillus niger
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
NADPH required
Aspergillus niger
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
iodoacetate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
N-ethylmaleimide
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
p-chloromercuribenzoate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
NADPH required
Aspergillus niger
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
-
Aspergillus niger
Ca2+
enzymes MGR I (slightly), MGR II
Aspergillus niger
Co2+
activates enzyme MGR I, slightly inhibits enzyme MGR II
Aspergillus niger
Cu2+
enzymes MGR I and MGR II
Aspergillus niger
dithiothreitol
-
Aspergillus niger
EDTA
-
Aspergillus niger
Glyoxal
in absence of NADPH
Aspergillus niger
iodoacetate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
methylglyoxal
in absence of NADPH
Aspergillus niger
Mg2+
enzymes MGR I and MGR II
Aspergillus niger
Mn2+
enzymes MGR I, MGR II
Aspergillus niger
N-ethylmaleimide
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
NADP+
-
Aspergillus niger
Ni2+
enzyme MGR I
Aspergillus niger
p-chloromercuribenzoate
activation of enzyme MGR I, inhibition of enzyme MGR II
Aspergillus niger
Phenylglyoxal
in absence of NADPH
Aspergillus niger
Zn2+
enzyme MGR I
Aspergillus niger
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0068
-
NADPH
enzyme MGR II
Aspergillus niger
0.054
-
NADPH
enzyme MGR I
Aspergillus niger
0.7
-
methylglyoxal
-
Aspergillus niger
1.43
-
methylglyoxal
enzyme MGR I
Aspergillus niger
4.35
-
Phenylglyoxal
enzyme MGR II
Aspergillus niger
10
-
Glyoxal
enzyme MGR II
Aspergillus niger
15.4
-
methylglyoxal
enzyme MGR I
Aspergillus niger
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
activates enzyme MGR I, slightly inhibits enzyme MGR II
Aspergillus niger
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
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
37000
-
enzyme MGR I, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration
Aspergillus niger
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methylglyoxal + NADPH
Aspergillus niger
similar enzyme with NADPH requirement
lactaldehyde + NADP+
-
Aspergillus niger
?
Purification (Commentary) (protein specific)
Commentary
Organism
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
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.83
-
enzyme MGR I
Aspergillus niger
7.77
-
enzyme MGR II
Aspergillus niger
Storage Stability (protein specific)
Storage Stability
Organism
4°C
Aspergillus niger
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + NADPH + H+
enzyme MGR II
207974
Aspergillus niger
ethanol + NADP+
-
207974
Aspergillus niger
?
glyoxal + NADPH
enzymes MGR I and MGR II
207974
Aspergillus niger
glycolaldehyde + NADP+
-
207974
Aspergillus niger
?
methylglyoxal + NADPH
similar enzyme with NADPH requirement
207974
Aspergillus niger
lactaldehyde + NADP+
-
207974
Aspergillus niger
?
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)
207974
Aspergillus niger
?
-
-
-
-
phenylglyoxal + NADPH
enzymes MGR I and MGR II
207974
Aspergillus niger
hydroxyphenylacetaldehyde + NADP+
-
207974
Aspergillus niger
?
propionaldehyde + NADPH
enzyme MGR II
207974
Aspergillus niger
propanol + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
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 (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
enzyme MGR I
Aspergillus niger
9
-
enzyme MGR II
Aspergillus niger
Other publictions for EC 1.1.1.283
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736122
Akita
Molecular cloning and characte ...
Kluyveromyces marxianus, Kluyveromyces marxianus DMB1
FEMS Microbiol. Lett.
362
fnv116
2015
-
-
1
-
-
-
-
4
-
-
3
-
-
9
-
-
-
-
-
-
11
-
26
1
2
-
2
4
1
-
-
2
-
-
-
-
-
2
4
-
-
-
-
-
-
4
-
-
4
-
-
-
-
-
-
-
11
-
26
2
2
-
4
4
2
-
-
-
-
-
-
-
-
-
737753
Guo
Structural insights into the c ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1844
1486-1492
2014
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741962
Guo
Structural insights into the ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1844
1486-1492
2014
-
-
1
1
1
-
-
-
-
-
-
2
-
2
-
-
1
1
-
-
-
-
5
1
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
1
1
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
5
1
1
-
-
-
1
-
-
-
-
3
3
-
-
-
710768
Breicha
Crystallization and preliminar ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
66
838-841
2010
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692329
Greig
A comparative study of methylg ...
Leishmania major, Leishmania major Friedlin, Trypanosoma brucei, Trypanosoma cruzi
FEBS J.
276
376-386
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
3
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686820
Hauser
A transcriptome analysis of is ...
Saccharomyces cerevisiae
FEMS Yeast Res.
7
84-92
2007
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670170
Xu
Methylglyoxal detoxification b ...
Synechococcus sp.
Microbiology
152
2013-2021
2006
-
-
-
-
-
-
-
11
-
-
-
-
-
3
-
-
-
-
-
-
17
-
18
-
-
-
-
11
1
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
17
-
18
-
-
-
-
11
1
-
1
-
-
-
-
-
-
-
739760
Warringer
Involvement of yeast YOL151W/G ...
Saccharomyces cerevisiae
Yeast
23
389-398
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
657418
Chen
Associating protein activities ...
Saccharomyces cerevisiae
Yeast
20
545-554
2003
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
738443
Rodriguez
Highly stereoselective reagent ...
Saccharomyces cerevisiae
J. Am. Chem. Soc.
123
1547-1555
2001
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
207977
Inoue
-
Purification and characterizat ...
Cyberlindnera mrakii
J. Ferment. Bioeng.
71
134-136
1991
-
-
-
-
-
-
3
2
-
-
1
1
-
1
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
2
-
-
1
1
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
207974
Inoue
Metabolism of 2-oxoaldehyde in ...
Aspergillus niger
Eur. J. Biochem.
171
213-218
1988
3
-
-
-
-
-
17
7
-
1
3
1
-
1
-
-
1
1
-
-
2
1
6
1
-
-
-
-
2
-
-
1
-
-
-
3
-
-
1
-
-
-
-
17
-
7
-
1
3
1
-
-
-
1
-
-
2
1
6
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
207973
Murata
-
Metabolism of alpha-ketoglutar ...
Saccharomyces cerevisiae
J. Ferment. Technol.
64
1-4
1986
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
207971
Murata
Metabolism of 2-oxoaldehyde in ...
Saccharomyces cerevisiae
Eur. J. Biochem.
151
631-636
1985
6
-
-
-
-
-
8
3
-
-
1
1
-
1
-
1
1
-
-
-
1
1
4
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
8
-
3
-
-
1
1
-
-
1
1
-
-
1
1
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
207972
Murata
Phenotypic character of the me ...
Saccharomyces cerevisiae
Appl. Environ. Microbiol.
50
1200-1207
1985
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-