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Information on EC 1.1.1.283 - methylglyoxal reductase (NADPH)
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1.1.1.283 methylglyoxal reductase (NADPH)IUBMB Comments
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 , hexane-2,5-dione and 3-chloro-1-phenylpropan-1-one . 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.
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The enzyme appears in viruses and cellular organisms
Synonyms
sakr1, nadph-dependent methylglyoxal reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MeGR
NADPH-dependent methylglyoxal reductase
YGL039w1
YGL039w2
additional information
-
enzyme displays also isovaleraldehyde reductase activity (EC 1.1.1.265)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
-
-
-
-
(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-
(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-
(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
catalytic mechanism involving Ser127, Tyr165, and Lys169, overview. In the first step, the hydroxyl groups of the Ser127 and Tyr165 residues form hydrogen bonds with the carbonyl oxygen of isovaleraldehyde, stabilizing its position. Subsequently, the hydroxyl group of Tyr165 donates a hydrogen to the carbonyl through deprotonation. Concomitantly, NADPH releases a hydrogen from the B-face of the nicotinamide ring onto the susceptible position of the carbonyl group. Thus, the carbonyl group is reduced to an alcohol group, and the isoamyl alcohol and NADP+ are produced. Upon reduction of the carbonyl group, the hydrogen bond between the side chain of Tyr165 and isoamyl alcohol is broken. With the redox state change, the conformation of NADP+ also may change, accompanied by the opening of the interdomain cleft for the release of the product
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
78310-66-4
-
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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
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 + 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
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
?
-
-
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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NATURAL SUBSTRATE
NATURAL 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
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
-
-
?
additional information
?
-
-
important role in the suppression of filamentation in response to isoamyl alcohol
-
-
?
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
activation of enzyme MGR I, inhibition of enzyme MGR II
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
activation of enzyme MGR I, inhibition of enzyme MGR II
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.047
2.1
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
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+
-
-
brenda
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-
-
brenda
wild type strains IWD72 and BY4741 and enzyme knockout mutants, knockout mutant forms large, invasive filaments, activity increases at 5-6 h of cultivation in the presence of 0.5% isoamyl alcohol and then quickly declines to become undetectable after 8 h
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, which includes various oxidoreductases, some isomerases and lyases
physiological function
additional information
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
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
-
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
Show AA Sequence and Transmembrane Helices (291 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
-
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
37000
38000
-
enzyme MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration
37000
-
enzyme MGR I, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
enzyme 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
monomer
monomer
-
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
6.6% carbohydrate, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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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
in complex with NADP, to 3.2 A resolution. Monoclinic space group P21, two Gre2 protomers per asymmetric unit
purified recombinant enzyme in apoform and in a complex with NADPH, X-ray diffraction structure determination and analysis at 2.0 A and 2.4 A, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F132A/V162A
the replacement of Phe132/Val162, with Ala results in the elevation of enzymatic activity toward isovaleraldehyde, probably via enlarging the pocket entrance
additional information
-
creation of a knockout mutant that forms large, invasive filaments
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
-
enzymic activity declined rapidly when pH values were higher than 7.5 or lower than 5
670170
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration, followed by ultrafiltration
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-
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
gene gre2, recombinant expression of His6-tagged type and mutant enzymes in Escherichia coli strain BL21(DE3)
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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