Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
-
-
r
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 + NADPH
lactaldehyde + NADP+
methylglyoxal + NADPH + H+
(R)-lactataldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH + H+
(S)-lactaldehyde + NADP+
-
-
r
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
?
-
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 + 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+

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+
-
-
-
?
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
?
-
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
?
-
-
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
brenda
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