Information on EC 1.1.1.283 - methylglyoxal reductase (NADPH)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.283
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RECOMMENDED NAME
GeneOntology No.
methylglyoxal reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-lactaldehyde + NADP+ = methylglyoxal + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylglyoxal degradation IV
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methylglyoxal degradation V
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Pyruvate metabolism
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Propanoate metabolism
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactaldehyde:NADP+ oxidoreductase
The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.
CAS REGISTRY NUMBER
COMMENTARY hide
78310-66-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 methylglyoxylate reductases: MGR I and MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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Manually annotated by BRENDA team
Hansenula mrakii
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Manually annotated by BRENDA team
strain Friedlin
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Manually annotated by BRENDA team
strain Friedlin
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Manually annotated by BRENDA team
strain PCC 7002
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrobenzaldehyde + NADPH
2-nitrobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
?
3-nitrobenzaldehyde + NADPH + H+
3-nitrobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
benzaldehyde + NADPH
benzyl alcohol + NADP+
show the reaction diagram
-
-
-
-
?
crotonaldehyde + NADPH
(2Z)-but-2-en-1-ol + NADP+
show the reaction diagram
-
-
-
-
?
D-arabinose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
D-galactose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
D-glucose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
D-xylose + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
diacetyl + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
-
-
-
-
?
glyoxal + NADPH
glycolaldehyde + NADP+
show the reaction diagram
isatin + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
isopentaldehyde + NADPH + H+
isopentanol + NADP+
show the reaction diagram
-
-
-
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
show the reaction diagram
methylglyoxal + NADPH + H+
(R)-lactataldehyde + NADP+
show the reaction diagram
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-
-
-
?
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
show the reaction diagram
methylglyoxal + NADPH + H+
lactaldehyde + NADP+
show the reaction diagram
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-
-
-
?
ninhydrin + NADPH
? + NADP+
show the reaction diagram
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-
-
-
?
phenylglyoxal + NADPH
hydroxyphenylacetaldehyde + NADP+
show the reaction diagram
propionaldehyde + NADPH
propanol + NADP+
show the reaction diagram
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enzyme MGR II
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-
?
succinic semialdehyde + NADPH
? + NADP+
show the reaction diagram
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methylglyoxal + NADPH
lactaldehyde + NADP+
show the reaction diagram
additional information
?
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important role in the suppression of filamentation in response to isoamyl alcohol
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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activates enzyme MGR I, slightly inhibits enzyme MGR II
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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-
Ca2+
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enzymes MGR I (slightly), MGR II
Co2+
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activates enzyme MGR I, slightly inhibits enzyme MGR II
Cu2+
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enzymes MGR I and MGR II
dithiothreitol
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-
Glyoxal
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in absence of NADPH
iodoacetate
methylglyoxal
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in absence of NADPH
Mg2+
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enzymes MGR I and MGR II
Mn2+
-
enzymes MGR I, MGR II
N-dodecanoylsarcosine
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-
N-ethylmaleimide
NADP+
Ni2+
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enzyme MGR I
p-chloromercuribenzoate
Phenylglyoxal
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in absence of NADPH
sodium cholate
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sodium dodecylsulfate
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Zn2+
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enzyme MGR I
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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activates
dithiothreitol
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activates
glutathione
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activates
iodoacetate
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activation of enzyme MGR I, inhibition of enzyme MGR II
L-cysteine
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activates
N-ethylmaleimide
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activation of enzyme MGR I, inhibition of enzyme MGR II
p-chloromercuribenzoate
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activation of enzyme MGR I, inhibition of enzyme MGR II
Triton X-100
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activates
Tween 80
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activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31
2-nitrobenzaldehyde
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1 mM
0.91
3-Nitrobenzaldehyde
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1 mM
0.85
4-Nitrobenzaldehyde
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1 mM
1.69
benzaldehyde
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1 mM
160
D-galactose
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50 mM
445
D-glucose
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50 mM
104
D-xylose
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50 mM
0.56
DL-glyceraldehyde
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1 mM
10
Glyoxal
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enzyme MGR II
1.33
isopentaldehyde
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1 mM
234
L-arabinose
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50 mM
0.08 - 15.4
methylglyoxal
0.0068 - 0.054
NADPH
1.54 - 4.35
Phenylglyoxal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.31
2-nitrobenzaldehyde
Synechococcus sp.
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1 mM
1.12
3-Nitrobenzaldehyde
Synechococcus sp.
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1 mM
1.24
4-Nitrobenzaldehyde
Synechococcus sp.
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1 mM
1.05
benzaldehyde
Synechococcus sp.
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1 mM
0.68
D-galactose
Synechococcus sp.
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50 mM
0.62
D-glucose
Synechococcus sp.
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50 mM
1.22
D-xylose
Synechococcus sp.
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50 mM
0.52
DL-glyceraldehyde
Synechococcus sp.
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1 mM
0.65
isopentaldehyde
Synechococcus sp.
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1 mM
1.27
L-arabinose
Synechococcus sp.
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50 mM
0.85
methylglyoxal
Synechococcus sp.
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1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0048
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at 25C, in 50 mM HEPES (pH 7.0)
0.0053
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at 25C, in 50 mM HEPES (pH 7.0)
0.0094
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at 25C, in 50 mM HEPES (pH 7.0)
0.038
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1 mM acetaldehyde as substrate
0.047
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1 mM crotonaldehyde as substrate; 1 mM isatin as substrate
0.048
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1 mM dihydroxyacetone as substrate
0.109
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50 mM D-glucose as substrate
0.211
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1 mM ninhydrin as substrate
0.225
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1 mM succinic semialdehyde as substrate
0.24
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50 mM D-galactose as substrate
0.364
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50 mM L-arabinose as substrate
0.373
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1 mM diacetyl as substrate
0.507
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1 mM DL-glyceraldehyde as substrate
0.641
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1 mM isopentaldehyde as substrate
0.651
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1 mM benzaldehyde as substrate
0.66
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50 mM D-xylose as substrate
0.83
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enzyme MGR I
1.072
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1 mM 3-nitrobenzaldehyde as substrate
1.091
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1 mM 4-nitrobenzaldehyde as substrate
1.206
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1 mM 2-nitrobenzaldehyde as substrate
1.278
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1 mM methylglyoxal as substrate
7.77
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enzyme MGR II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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enzyme MGR I
9
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enzyme MGR II
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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gel filtration, SDS-PAGE
37000
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enzyme MGR I, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration
38000
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enzyme MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration
43000
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gel filtration, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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6.6% carbohydrate, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
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enzymic activity declined rapidly when pH values were higher than 7.5 or lower than 5
670170
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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two methylglyoxylate reductases: MGR I and MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
creation of a knockout mutant that forms large, invasive filaments
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