1.1.1.283: methylglyoxal reductase (NADPH)
This is an abbreviated version!
For detailed information about methylglyoxal reductase (NADPH), go to the full flat file.
Word Map on EC 1.1.1.283
Reaction
Synonyms
AKR, aldo-keto reductase, AlrA, CaGre2, CANTEDRAFT_112488, D-lactaldehyde dehydrogenase, EC 1.1.1.78, Gre2, GRE2 gene product, GRE2/YOL151W, Gre2p, GRE3, GRP2, Lbuc_0522, MeGR, Mer, methylglyoxal reductase, methylglyoxal reductase (NADPH dependent), methylglyoxal/isovaleraldehyde reductase, MG reductase, MG-specific aldolase reductase, MGR, More, NADPH-dependent methylglyoxal reductase, NADPH-linked aldolase reductase, PAS_chr3_0744, SakR1, YGL039w1, YGL039w2, YOL151W, YOL151w gene product
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1.1.1.283 methylglyoxal reductase (NADPH)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.1.1.283 - methylglyoxal reductase (NADPH)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
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
-
?
p-anisaldehyde + NADPH + H+
p-anisalcohol + NADP+
-
-
-
ir
pentanal + NADPH + H+
pentan-1-ol + NADP+
-
-
-
ir
valeraldehyde + NADPH + H+
amyl alcohol + NADP+
-
-
-
ir
(S)-lactaldehyde + NADP+
methylglyoxal + NADPH + H+
-
-
-
-
?
glyoxal + NADPH
glycolaldehyde + NADP+
-
enzymes MGR I and MGR II
-
?
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
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+
-
similar enzyme with NADPH requirement, no reaction with NAD+, NADH and NADP+
-
ir
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+
-
-
-
?
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
?
-
-
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
-
-
?
