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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Propanoate metabolism
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Pyruvate 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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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in strains lacking Gre2 activity, which are subjected to environmental stress straining the cell membrane, growth is significantly and exclusively reduced. No compensatory mechanisms are activated due to loss of Gre2p during growth in favourable conditions (synthetic defined media, no stress), but a striking and highly specific induction of the ergosterol biosynthesis pathway, enzymes Erg10, Erg19 and Erg6, is observed in Gre2 mutant strains during growth in a stress conditions in which lack of Gre2 significantly affects growth. Mutant strains display vastly impaired tolerance exclusively to agents targeting the ergosterol biosynthesis
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
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-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
show the reaction diagram
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-
-
-
?
DL-glyceraldehyde + NADPH
glycerol + NADP+
show the reaction diagram
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-
-
-
?
ethyl (2R)-2-methyl-3-oxobutanoate + NADPH + H+
ethyl (2R,3S)-3-hydroxy-2-methylbutanoate + NADP+
show the reaction diagram
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86% yield, 70% (2R,3S)-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
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?
ethyl 3-oxobutanoate + NADPH + H+
ethyl (3S)-3-hydroxybutanoate + NADP+
show the reaction diagram
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83% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
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?
ethyl 3-oxohexanoate + NADPH + H+
ethyl (3S)-3-hydroxyhexanoate + NADP+
show the reaction diagram
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90% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
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?
ethyl 3-oxopentanoate + NADPH + H+
ethyl (3S)-3-hydroxypentanoate + NADP+
show the reaction diagram
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87% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
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?
glyoxal + NADPH
glycolaldehyde + NADP+
show the reaction diagram
heptanal + NADPH + H+
heptan-1-ol + NADP+
show the reaction diagram
isatin + NADPH
? + NADP+
show the reaction diagram
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-
-
-
?
isopentaldehyde + NADPH + H+
isopentanol + NADP+
show the reaction diagram
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-
-
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?
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
show the reaction diagram
methyl 3-oxobutanoate + NADPH + H+
methyl (3S)-3-hydroxybutanoate + NADP+
show the reaction diagram
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76% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
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?
methyl 3-oxopentanoate + NADPH + H+
methyl (3S)-3-hydroxypentanoate + NADP+
show the reaction diagram
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85% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
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?
methyl glyoxal + NADPH + H+
? + 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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-
-
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?
octanal + NADPH + H+
octan-1-ol+ NADP+
show the reaction diagram
p-anisaldehyde + NADPH + H+
p-anisalcohol + NADP+
show the reaction diagram
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ir
pentanal + NADPH + H+
pentan-1-ol + NADP+
show the reaction diagram
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ir
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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?
valeraldehyde + NADPH + H+
isoamyl alcohol + NADP+
show the reaction diagram
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ir
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
additional information
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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+
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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
0.43 - 1.6
methyl glyoxal
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
2.5 - 4
methyl glyoxal
0.85
methylglyoxal
Synechococcus sp.
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1 mM
2.67 - 3.67
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0048
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at 25°C, in 50 mM HEPES (pH 7.0)
0.0053
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at 25°C, in 50 mM HEPES (pH 7.0)
0.0094
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at 25°C, 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
0.96
substrate methylglyoxal, pH 6.0, 25°C
1.072
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1 mM 3-nitrobenzaldehyde as substrate
1.091
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1 mM 4-nitrobenzaldehyde as substrate
1.1
substrate p-anisaldehyde, pH 6.0, 25°C
1.206
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1 mM 2-nitrobenzaldehyde as substrate
1.278
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1 mM methylglyoxal as substrate
2.1
substrate octanal, pH 6.0, 25°C; substrate valeraldehyde, pH 6.0, 25°C
3
substrate heptanal, pH 6.0, 25°C
3.2
substrate methyl glyoxal, pH 6.0, 25°C
3.3
substrate isovaleraldehyde, pH 6.0, 25°C
4.2
substrate isovaleraldehyde, pH 6.0, 25°C
4.5
substrate p-anisaldehyde, pH 6.0, 25°C
5.3
substrate octanal, pH 6.0, 25°C
5.9
substrate valeraldehyde, pH 6.0, 25°C
6.9
substrate heptanal, pH 6.0, 25°C
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
36000
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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
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+
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures in an apo-form at 2.00 A and NADPH-complexed form at 2.40 A resolution. 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
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in complex with NADP, to 3.2 A resolution. Monoclinic space group P21, two Gre2 protomers per asymmetric unit
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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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
below 40°C, 30 min, 80% residual activity; below 40°C, 30 min, 80% residual activity
50
30 min, 26% residual activity; 30 min, complete loss of activity
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
expression in Escherichia coli
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expression in Escherichia coli; expression in Escherichia coli
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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engineeering of Sacharomyces cerevisiae for specific reduction of a variety of carbonyl compounds by altering the levels of fatty acid synthase Fas, aldo-keto reductase Ypr1 and R-acetoxy ketone reductase Gre2. By choosing the appropriate engineered yeast strain, it is possible to prepare many of the alcohols in high stereochemical purities and good chemical yields. For example, in the reductions of some alpha-unsubstituted beta-keto esters, genetically disabling Fas virtually eliminates production of (3R)-alcohols. Overexpressing (3S)-selective reductase Gre2 in the Fas knockout strain gives yeast cells that reduce these ketones to the corresponding (3S)-alcohols in >98% ee in each case
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