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(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
2-nitrobenzaldehyde + NADPH
2-nitrobenzyl alcohol + NADP+
-
-
-
-
?
3-nitrobenzaldehyde + NADPH + H+
3-nitrobenzyl alcohol + NADP+
-
-
-
-
?
4-nitrobenzaldehyde + NADPH + H+
4-nitrobenzyl alcohol + NADP+
-
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
benzaldehyde + NADPH
benzyl alcohol + NADP+
-
-
-
-
?
crotonaldehyde + NADPH
(2Z)-but-2-en-1-ol + NADP+
-
-
-
-
?
D-arabinose + NADPH
? + NADP+
-
-
-
-
?
D-galactose + NADPH
? + NADP+
-
-
-
-
?
D-glucose + NADPH
? + NADP+
-
-
-
-
?
D-xylose + NADPH
? + NADP+
-
-
-
-
?
diacetyl + NADPH
? + NADP+
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
?
DL-glyceraldehyde + NADPH
glycerol + NADP+
-
-
-
-
?
ethyl (2R)-2-methyl-3-oxobutanoate + NADPH + H+
ethyl (2R,3S)-3-hydroxy-2-methylbutanoate + NADP+
-
86% yield, 70% (2R,3S)-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
-
?
ethyl 3-oxobutanoate + NADPH + H+
ethyl (3S)-3-hydroxybutanoate + NADP+
-
83% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
-
?
ethyl 3-oxohexanoate + NADPH + H+
ethyl (3S)-3-hydroxyhexanoate + NADP+
-
90% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
-
?
ethyl 3-oxopentanoate + NADPH + H+
ethyl (3S)-3-hydroxypentanoate + NADP+
-
87% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
-
?
glyoxal + NADPH
glycolaldehyde + NADP+
heptanal + NADPH + H+
heptan-1-ol + NADP+
isatin + NADPH
? + NADP+
-
-
-
-
?
isopentaldehyde + NADPH + H+
isopentanol + NADP+
-
-
-
-
?
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
L-arabinose + NADPH + H+
?
-
-
-
-
r
methyl 3-oxobutanoate + NADPH + H+
methyl (3S)-3-hydroxybutanoate + NADP+
-
76% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
-
?
methyl 3-oxopentanoate + NADPH + H+
methyl (3S)-3-hydroxypentanoate + NADP+
-
85% yield, 98% S-enantiomer in a strain lacking fatty acid synthase activity and overexpressing Gre2
-
?
methyl glyoxal + NADPH + H+
? + NADP+
methylglyoxal + NADH + H+
(S)-lactaldehyde + NAD+
methylglyoxal + NADPH
lactaldehyde + NADP+
methylglyoxal + NADPH + H+
(R)-lactataldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
lactaldehyde + NADP+
ninhydrin + NADPH
? + NADP+
-
-
-
-
?
octanal + NADPH + H+
octan-1-ol + NADP+
p-anisaldehyde + NADPH + H+
p-anisalcohol + NADP+
-
-
-
ir
pentanal + NADPH + H+
pentan-1-ol + NADP+
-
-
-
ir
phenylglyoxal + NADPH
hydroxyphenylacetaldehyde + NADP+
propionaldehyde + NADPH
propanol + NADP+
-
enzyme MGR II
-
-
?
succinic semialdehyde + NADPH
? + NADP+
-
-
-
-
?
valeraldehyde + NADPH + H+
amyl alcohol + NADP+
-
-
-
ir
additional information
?
-
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
-
-
-
?
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
-
-
-
-
?
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
-
-
-
-
?
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
-
-
-
r
acetaldehyde + NADPH + H+
ethanol + NADP+
-
enzyme MGR II
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
-
?
glyoxal + NADPH
glycolaldehyde + NADP+
-
enzymes MGR I and MGR II
-
?
glyoxal + NADPH
glycolaldehyde + NADP+
-
-
-
ir
heptanal + NADPH + H+
heptan-1-ol + NADP+
-
-
-
ir
heptanal + NADPH + H+
heptan-1-ol + NADP+
-
-
-
ir
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
-
-
-
ir
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
-
-
-
ir
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
catalytic mechanism involving Ser127, Tyr165, and Lys169, overview. The carbonyl oxygen interactswith the side chain of Ser127, Tyr165 through hydrogen bonds (about 2.7 A), giving a distance of 3.0 A between the C4 atom of the nicotinamide and the carbonyl carbon of substrate
-
-
?
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
catalytic mechanism involving Ser127, Tyr165, and Lys169, overview. The carbonyl oxygen interacts with the side chain of Ser127, Tyr165 through hydrogen bonds (about 2.7 A), giving a distance of 3.0 A between the C4 atom of the nicotinamide and the carbonyl carbon of substrate
-
-
?
methyl glyoxal + NADPH + H+
? + NADP+
-
-
-
ir
methyl glyoxal + NADPH + H+
? + NADP+
-
-
-
ir
methylglyoxal + NADH + H+
(S)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADH + H+
(S)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
similar enzyme with NADPH requirement
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
similar enzyme with NADPH requirement
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
similar enzyme with NADPH requirement, no reaction with NAD+, NADH and NADP+
-
ir
methylglyoxal + NADPH
lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
r
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
-
-
-
-
r
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
L-lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
lactaldehyde + NADP+
-
-
-
-
?
methylglyoxal + NADPH + H+
lactaldehyde + NADP+
-
-
-
-
?
octanal + NADPH + H+
octan-1-ol + NADP+
-
-
-
ir
octanal + NADPH + H+
octan-1-ol + NADP+
-
-
-
ir
phenylglyoxal + NADPH
hydroxyphenylacetaldehyde + NADP+
-
enzymes MGR I and MGR II
-
?
phenylglyoxal + NADPH
hydroxyphenylacetaldehyde + NADP+
-
-
-
?
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)
-
-
?
additional information
?
-
CaGre2 exhibits a stronger affinity for NADPH than NADH
-
-
-
additional information
?
-
CaGre2 exhibits a stronger affinity for NADPH than NADH
-
-
-
additional information
?
-
methylglyoxal-specific aldolase reductase activity
-
-
-
additional information
?
-
-
methylglyoxal-specific aldolase reductase activity
-
-
-
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
-
enzyme shows strong activities toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as heptanal, valeraldehyde and octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as heptanal, valeraldehyde and octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
-
enzyme shows strong activities toward linear aldehydes, such as heptanal, valeraldehyde and octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as 1-heptanal, valeraldehyde and 1-octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as heptanal, valeraldehyde and octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
enzyme shows strong activities toward linear aldehydes, such as heptanal, valeraldehyde and octanal, but no activity toward HMF, propionaldehyde, D-alanine, L-alanine, D-lactate, L-lactate or pyruvate. Enzyme has no NADP+-dependent oxidative activity toward corresponding alcohol analogs, including 1-hexanol, 1-heptanol, isoamyl alcohol, isobutanol, 1-octanol and 2-propanol
-
-
?
additional information
?
-
-
recombinantly overexpressed F420-dependent N5,N10-methylenetetrahydromethanopterin reductase Mer, EC 1.5.98.2, is able to use NADPH and methylglyoxal to produce lactaldehyde. Mer does not catalyze the reduction of methylglyoxal to lactaldehyde in the presence of reduced Fo, the precursor of cofactor F420
-
-
-
additional information
?
-
-
NADPH required
-
-
?
additional information
?
-
-
important role in the suppression of filamentation in response to isoamyl alcohol
-
-
?
additional information
?
-
-
enzyme displays also isovaleraldehyde reductase activity (EC 1.1.1.265)
-
-
?
additional information
?
-
the substrate recognition and the catalytic mechanism underlie the stereoselective reduction of Gre2. Analysis of the substrate-binding site using computational simulation and enzymatic activity assays, noticeable induced fit upon NADPH binding, overview. In Gre2, the hydrophobic residues Phe85, Tyr128 and Tyr198 combine with Phe132 and Val162 to form one funneled pocket which consists of one broad pocket entrance and one deep hydrophobic channel. The extended hydrophobic entrance of Gre2 plays a role in accommodating a wide variety of carbonyl compounds, such as diketones, aliphatic and cyclic alpha- and beta-keto esters and aldehydes.The deep hydrophobic channel prefers to identify a substrate with a linear substrate. That is why Gre2 shows high reduction activity to butanal, pentanal and 2,5-hexanedione, as well as some aldehydes
-
-
?
additional information
?
-
-
the substrate recognition and the catalytic mechanism underlie the stereoselective reduction of Gre2. Analysis of the substrate-binding site using computational simulation and enzymatic activity assays, noticeable induced fit upon NADPH binding, overview. In Gre2, the hydrophobic residues Phe85, Tyr128 and Tyr198 combine with Phe132 and Val162 to form one funneled pocket which consists of one broad pocket entrance and one deep hydrophobic channel. The extended hydrophobic entrance of Gre2 plays a role in accommodating a wide variety of carbonyl compounds, such as diketones, aliphatic and cyclic alpha- and beta-keto esters and aldehydes.The deep hydrophobic channel prefers to identify a substrate with a linear substrate. That is why Gre2 shows high reduction activity to butanal, pentanal and 2,5-hexanedione, as well as some aldehydes
-
-
?
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malfunction
glutathione (GSH)-deprived Dictyostelium discoideum accumulates methylglyoxal (MG) and reactive oxygen species (ROS) during vegetative growth. MG increases after the mound stage in this strain, with a 2.6fold increase compared to early developmental stages. gamma-Glutamylcysteine synthetase overexpressing (gcsAOE) slugs trigger glutahione reductase (Gsr) and aldolase reductase activity to detoxify MG, while superoxide dismutase overexpressing (sod2OE) and catalase overexpressing (catAOE) slugs mainly decrease cellular ROS levels. The MG-specific activity of NADPH-linked aldolase reductase shows a noticeable increase in the gcsAOE slugs, indicating enhanced MG-scavenging reductase activity in gcsAOE slugs. In contrast to the increase observed in migrating sod2OE and catAOE slugs by treatment with MG and H2O2, the migration of gcsAOE slugs appeas unaffected. This behavior is caused by MG-triggered Gsr and NADPH-linked aldolase reductase activity, suggesting that GSH biosynthesis in gcsAOE slugs is specifically used for MG-scavenging activity
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, which includes various oxidoreductases, some isomerases and lyases
evolution
-
MG reductases are highly conserved
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
evolution
-
the organism contains 1 MGR gene copy
evolution
-
the organism contains 2 MGR gene copies
evolution
the organism contains 2 MGR gene copies
evolution
-
the organism contains 3 MGR gene copies
evolution
-
the organism contains 3 MGR gene copies
evolution
-
the organism contains 4 MGR gene copies
evolution
-
the organism contains 4 MGR gene copies
evolution
the organism contains 4 MGR gene copies
evolution
-
the organism contains 5 MGR gene copies
evolution
the organism contains 6 MGR gene copies
evolution
-
the organism contains 7 MGR gene copies
evolution
-
the organism contains 8 MGR gene copies
evolution
the organism contains 9 MGR gene copies
evolution
-
the organism contains diverse MGR gene copies
evolution
-
the organism contains 2 MGR gene copies
-
evolution
-
MG reductases are highly conserved
-
evolution
-
the organism contains 2 MGR gene copies
-
evolution
-
the organism contains 2 MGR gene copies
-
evolution
-
the organism contains 6 MGR gene copies
-
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
-
evolution
-
the organism contains 4 MGR gene copies
-
evolution
-
the organism contains 2 MGR gene copies
-
evolution
-
the organism contains 2 MGR gene copies
-
evolution
-
the organism contains 6 MGR gene copies
-
evolution
-
the organism contains 2 MGR gene copies
-
evolution
-
the organism contains 2 MGR gene copies
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
physiological function
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
physiological function
the Saccharomyces cerevisiae enzyme serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor
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
physiological function
methylglyoxal (MG) upregulates slug migration via MG-scavenging-mediated differentiation
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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model for MGR role in oxidative imbalance, overview
physiological function
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the enzyme is involved in detoxification of methylglyoxal (MG), a cytotoxic by-product of glycolysis that is identified as a potential glycolytic inhibitor, which inhibits the growth of glucose-fermenting yeast cells by promoting degradation of the glucose sensors. The MG reductase gene has been reported to play a critical role in maintaining redox balance during ethanol fermentation in yeasts
physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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the enzyme is involved in detoxification of methylglyoxal (MG), a cytotoxic by-product of glycolysis that is identified as a potential glycolytic inhibitor, which inhibits the growth of glucose-fermenting yeast cells by promoting degradation of the glucose sensors. The MG reductase gene has been reported to play a critical role in maintaining redox balance during ethanol fermentation in yeasts
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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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
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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physiological function
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model for MGR role in oxidative imbalance, overview
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additional information
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. The substrate-binding pocket structure determines the stringent substrate stereoselectivity for catalysis
additional information
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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. The substrate-binding pocket structure determines the stringent substrate stereoselectivity for catalysis
additional information
enzyme sequence and structure comparisons, overview
additional information
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evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
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evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
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evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
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evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
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additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
enzyme sequence and structure comparisons, overview
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
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Murata, K.; Fukuda, Y.; Simosaka, M.; Watanabe, K.; Saikusa, T.; Kimura, A.
Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae
Eur. J. Biochem.
151
631-636
1985
Saccharomyces cerevisiae
brenda
Murata, K.; Fukuda, Y.; Shimosaka, M.; Watanabe, K.; Saikusa, T.; Kimura, A.
Phenotypic character of the methylglyoxal resistance gene in Saccharomyces cerevisiae: expression in Escherichia coli and application to breeding wild-type yeast strains
Appl. Environ. Microbiol.
50
1200-1207
1985
Saccharomyces cerevisiae
brenda
Murata, K.; Inoue, Y.; Saikusa, T.; Watanabe, K.; Fukuda, Y.; Shimosaka, M.; Kimura, A.
Metabolism of alpha-ketoglutarate in yeasts: inducible formation of methylglyoxal reductase and its relation to growth arrest of Saccharomyces cerevisiae
J. Ferment. Technol.
64
1-4
1986
Saccharomyces cerevisiae
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brenda
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
Eur. J. Biochem.
171
213-218
1988
Aspergillus niger
brenda
Inoue, Y.; Tran Linh, T.; Yoshikawa, K.; Murata, K.; Kimura, A.
Purification and characterization of methylglyoxal reductase from Hansenula mrakii
J. Ferment. Bioeng.
71
134-136
1991
Cyberlindnera mrakii
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brenda
Chen, C.N.; Porubleva, L.; Shearer, G.; Svrakic, M.; Holden, L.G.; Dover, J.L.; Johnston, M.; Chitnis, P.R.; Kohl, D.H.
Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae
Yeast
20
545-554
2003
Saccharomyces cerevisiae
brenda
Xu, D.; Liu, X.; Guo, C.; Zhao, J.
Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002
Microbiology
152
2013-2021
2006
Synechococcus sp.
brenda
Hauser, M.; Horn, P.; Tournu, H.; Hauser, N.C.; Hoheisel, J.D.; Brown, A.J.; Dickinson, J.R.
A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase
FEMS Yeast Res.
7
84-92
2007
Saccharomyces cerevisiae
brenda
Greig, N.; Wyllie, S.; Patterson, S.; Fairlamb, A.H.
A comparative study of methylglyoxal metabolism in trypanosomatids
FEBS J.
276
376-386
2009
Leishmania major, Trypanosoma brucei, Trypanosoma cruzi, Leishmania major Friedlin
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Breicha, K.; Mueller, M.; Hummel, W.; Niefind, K.
Crystallization and preliminary crystallographic analysis of Gre2p, an NADP(+)-dependent alcohol dehydrogenase from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
66
838-841
2010
Saccharomyces cerevisiae (Q12068)
brenda
Akita, H.; Watanabe, M.; Suzuki, T.; Nakashima, N.; Hoshino, T.
Molecular cloning and characterization of two YGL039w genes encoding broad specificity NADPH-dependent aldehyde reductases from Kluyveromyces marxianus strain DMB1
FEMS Microbiol. Lett.
362
fnv116
2015
Kluyveromyces marxianus (A0A0E4AX59), Kluyveromyces marxianus (A0A0E4AY21), Kluyveromyces marxianus, Kluyveromyces marxianus DMB1 (A0A0E4AX59), Kluyveromyces marxianus DMB1 (A0A0E4AY21)
brenda
Guo, P.C.; Bao, Z.Z.; Ma, X.X.; Xia, Q.; Li, W.F.
Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2
Biochim. Biophys. Acta
1844
1486-1492
2014
Saccharomyces cerevisiae (Q12068), Saccharomyces cerevisiae
brenda
Rodriguez, S.; Kayser, M.M.; Stewart, J.D.
Highly stereoselective reagents for beta-keto ester reductions by genetic engineering of bakers yeast
J. Am. Chem. Soc.
123
1547-1555
2001
Saccharomyces cerevisiae (Q12068)
brenda
Warringer, J.; Blomberg, A.
Involvement of yeast YOL151W/GRE2 in ergosterol metabolism
Yeast
23
389-398
2006
Saccharomyces cerevisiae (Q12068)
brenda
Guo, P.C.; Bao, Z.Z.; Ma, X.X.; Xia, Q.; Li, W.F.
Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2
Biochim. Biophys. Acta
1844
1486-1492
2014
Saccharomyces cerevisiae (Q12068), Saccharomyces cerevisiae
brenda
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
Crystals
9
471
2019
Candida albicans (A0A1D8PHQ6), Candida albicans ATCC MYA-2876 (A0A1D8PHQ6)
-
brenda
Borelli, G.; Fiamenghi, M.B.; Dos Santos, L.V.; Carazzolle, M.F.; Pereira, G.A.G.; Jose, J.
Positive selection evidence in xylose-related genes suggests methylglyoxal reductase as a target for the improvement of yeasts fermentation in industry
Genome Biol. Evol.
11
1923-1938
2019
Blastobotrys adeninivorans, [Candida] boidinii, Wickerhamomyces anomalus, Candida tropicalis, Kluyveromyces lactis, Lipomyces starkeyi, no activity in Schizosaccharomyces pombe, [Candida] arabinofermentans, no activity in Dekkera bruxellensis, Candida sojae, Suhomyces tanzawaensis, Kazachstania africana, Yarrowia lipolytica (A0A1D8NEA1), Komagataella phaffii (C4R5F8), Yamadazyma tenuis (G3AZL9), Saccharomyces cerevisiae (P38715), Saccharomyces cerevisiae (Q12068), Yamadazyma tenuis VKM Y-70 (G3AZL9), Yamadazyma tenuis BCRC 21748 (G3AZL9), Yamadazyma tenuis CBS 615 (G3AZL9), Komagataella phaffii ATCC 20864 (C4R5F8), Saccharomyces cerevisiae ATCC 204508 (P38715), Saccharomyces cerevisiae ATCC 204508 (Q12068), Yamadazyma tenuis NBRC 10315 (G3AZL9), Yamadazyma tenuis ATCC 10573 (G3AZL9), Komagataella phaffii GS115 (C4R5F8), Yamadazyma tenuis JCM 9827 (G3AZL9), Yamadazyma tenuis NRRL Y-1498 (G3AZL9)
brenda
Lee, H.M.; Seo, J.H.; Kwak, M.K.; Kang, S.O.
Methylglyoxal upregulates Dictyostelium discoideum slug migration by triggering glutathione reductase and methylglyoxal reductase activity
Int. J. Biochem. Cell Biol.
90
81-92
2017
Dictyostelium discoideum (Q6IMN8), Dictyostelium discoideum
brenda
Liu, S.; Skory, C.; Qureshi, N.
Ethanol tolerance assessment in recombinant E. coli of ethanol responsive genes from Lactobacillus buchneri NRRL B-30929
World J. Microbiol. Biotechnol.
36
179
2020
Lentilactobacillus buchneri, Lentilactobacillus buchneri NRRL B-30929
brenda
Miller, D.; Ruhlin, M.; Ray, W.; Xu, H.; White, R.
N5,N10-methylenetetrahydromethanopterin reductase from Methanocaldococcus jannaschii also serves as a methylglyoxal reductase
FEBS Lett.
591
2269-2278
2017
Methanocaldococcus jannaschii
brenda