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EC Tree
IUBMB Comments The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.
The enzyme appears in viruses and cellular organisms
Synonyms
yol151w, gre2p, ymr152wp, ymr152w, 3-methylbutanal reductase, isovaleraldehyde reductase, branched-chain alcohol dehydrogenase, gre2 gene product,
more
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3-methylbutyraldehyde reductase
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branched-chain alcohol dehydrogenase
-
-
isoamylaldehyde reductase
-
-
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-
isopentanal reductase
-
-
-
-
isovaleral reductase
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-
-
-
isovaleraldehyde reductase
additional information
-
enzyme displays also NADPH dependent methylglyoxal reductase activity (EC 1.1.1.283)
aldehyde reductase
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isovaleraldehyde reductase
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isovaleraldehyde reductase
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protein YIM1
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YIM1
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YMR152W
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Ymr152wp
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3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+
The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes
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3-methylbutanol:NAD(P)+ oxidoreductase
The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.
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2,3-pentanedione + NAD(P)H
? + NAD(P)+
-
very low activity
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?
2-methylbutanal + NAD(P)H
2-methylbutanol + NAD(P)+
-
-
-
r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
3-methylbutanal + NAD(P)H + H+
3-methylbutanol + NAD(P)+
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-
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r
3-methylbutanal + NADH + H+
3-methylbutanol + NAD+
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-
-
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r
3-methylbutanal + NADPH + H+
3-methylbutanol + NADP+
3-methylthiopropionaldehyde + NADPH + H+
3-methylthiopropanol + NADP+
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specific substrate for Sacchaormyces cerevisiae, main contribution to the strong worty flavor of alcohol-free beer
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?
3-pyridine carboxaldehyde + NAD(P)H
3-pyridinemethanol + NAD(P)+
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highest activity
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?
5-hydroxymethylfurfural + NADH + H+
2,5-dihydroxymethylfurane + NAD+
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-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
acetaldehyde + NADPH + H+
ethanol + NADP+
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
butanal + NAD(P)H + H+
butanol + NAD(P)+
-
-
-
r
diacetyl + NAD(P)H
? + NAD(P)+
furaldehyde + NAD(P)H
furfuryl alcohol + NAD(P)+
furfural + NADH + H+
furfuryl alcohol + NAD+
gluconate + NAD(P)H
D-glucose + NAD(P)+
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very low activity in both reduction and oxidation
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r
glyceraldehyde + NAD(P)H
glycerol + NAD(P)+
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?
glycolaldehyde + NADH + H+
ethylene glycol + NAD+
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r
heptanal + NADPH
heptanol + NADP+
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preference for long and branched-chain substrates with up to seven carbon atoms
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r
hexanal + NADPH + H+
hexanol + NADP+
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
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important role in the suppression of filamentation in response to isoamyl alcohol/isovaleraldehyde
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-
r
methyl glyoxal + NAD(P)H
? + NAD(P)+
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low activity
-
?
octanal + NAD(P)H + H+
octanol + NAD(P)+
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-
-
?
p-anisaldehyde + NAD(P)H
p-anisalcohol + NAD(P)+
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20-50% of the activity with 3-methylbutanal for aromatic aldehydes
-
?
pentanal + NADPH
pentanol + NADP+
propanal + NAD(P)H + H+
propanol + NAD(P)+
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-
-
r
trans-2-hexenol + NADP+
trans-2-hexenal + NADPH
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-
-
?
additional information
?
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3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
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r
3-methylbutanal + NADPH + H+
3-methylbutanol + NADP+
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-
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r
3-methylbutanal + NADPH + H+
3-methylbutanol + NADP+
low activity
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-
r
acetaldehyde + NADH + H+
ethanol + NAD+
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-
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r
acetaldehyde + NADH + H+
ethanol + NAD+
best substrate
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-
r
acetaldehyde + NADH + H+
ethanol + NAD+
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r
acetaldehyde + NADH + H+
ethanol + NAD+
best substrate
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r
acetaldehyde + NADPH + H+
ethanol + NADP+
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r
acetaldehyde + NADPH + H+
ethanol + NADP+
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-
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r
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
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high activity
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?
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
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20-50% of the activity with 3-methylbutanal for aromatic aldehydes
-
?
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
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-
-
r
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
low activity
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r
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
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-
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r
diacetyl + NAD(P)H
? + NAD(P)+
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very low activity
-
?
diacetyl + NAD(P)H
? + NAD(P)+
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very low activity
-
?
furaldehyde + NAD(P)H
furfuryl alcohol + NAD(P)+
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-
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?
furaldehyde + NAD(P)H
furfuryl alcohol + NAD(P)+
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20-50% of the activity with 3-methylbutanal for aromatic aldehydes
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?
furfural + NADH + H+
furfuryl alcohol + NAD+
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-
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r
furfural + NADH + H+
furfuryl alcohol + NAD+
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r
hexanal + NADPH + H+
hexanol + NADP+
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r
hexanal + NADPH + H+
hexanol + NADP+
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r
pentanal + NADPH
pentanol + NADP+
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r
pentanal + NADPH
pentanol + NADP+
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r
additional information
?
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enzyme displays also NADPH dependent methylglyoxal reductase activity (EC 1.1.1.283)
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?
additional information
?
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Ymr152wp catalyzes reactions for reduction of acetaldehyde, glycolaldehyde, furfural, and 5-hydroxymethylfurfural (HMF) when NADH is used as the cofactor. Besides, enzyme activity is detected for reduction of benzaldehyde (BZA) and 3-methylbutanal (MBA) when NADPH is used as the cofactor. Ymr152wp shows the highest specific enzyme activity (190.86 U/mg) for reduction of acetaldehyde, followed by glycolaldehyde (9.64 U/mg), furfural (5.05 U/mg), HMF (1.74 U/mg), BZA (1.12 U/mg), and MBA (0.74 U/mg). No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, quinone, 1,2-naphthoquinone, 9,10-phenanthrenequinone, 4-benzoquinone, acetone, and acetylacetone, neither with NADH, nor with NADPH
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additional information
?
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Ymr152wp catalyzes reactions for reduction of acetaldehyde, glycolaldehyde, furfural, and 5-hydroxymethylfurfural (HMF) when NADH is used as the cofactor. Besides, enzyme activity is detected for reduction of benzaldehyde (BZA) and 3-methylbutanal (MBA) when NADPH is used as the cofactor. Ymr152wp shows the highest specific enzyme activity (190.86 U/mg) for reduction of acetaldehyde, followed by glycolaldehyde (9.64 U/mg), furfural (5.05 U/mg), HMF (1.74 U/mg), BZA (1.12 U/mg), and MBA (0.74 U/mg). No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, quinone, 1,2-naphthoquinone, 9,10-phenanthrenequinone, 4-benzoquinone, acetone, and acetylacetone, neither with NADH, nor with NADPH
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additional information
?
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Ymr152wp catalyzes reactions for reduction of acetaldehyde, glycolaldehyde, furfural, and 5-hydroxymethylfurfural (HMF) when NADH is used as the cofactor. Besides, enzyme activity is detected for reduction of benzaldehyde (BZA) and 3-methylbutanal (MBA) when NADPH is used as the cofactor. Ymr152wp shows the highest specific enzyme activity (190.86 U/mg) for reduction of acetaldehyde, followed by glycolaldehyde (9.64 U/mg), furfural (5.05 U/mg), HMF (1.74 U/mg), BZA (1.12 U/mg), and MBA (0.74 U/mg). No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, quinone, 1,2-naphthoquinone, 9,10-phenanthrenequinone, 4-benzoquinone, acetone, and acetylacetone, neither with NADH, nor with NADPH
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3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
3-methylbutanal + NADPH + H+
3-methylbutanol + NADP+
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r
5-hydroxymethylfurfural + NADH + H+
2,5-dihydroxymethylfurane + NAD+
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-
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r
acetaldehyde + NADH + H+
ethanol + NAD+
acetaldehyde + NADPH + H+
ethanol + NADP+
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
furfural + NADH + H+
furfuryl alcohol + NAD+
gluconate + NAD(P)H
D-glucose + NAD(P)+
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very low activity in both reduction and oxidation
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r
glyceraldehyde + NAD(P)H
glycerol + NAD(P)+
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?
glycolaldehyde + NADH + H+
ethylene glycol + NAD+
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-
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r
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
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important role in the suppression of filamentation in response to isoamyl alcohol/isovaleraldehyde
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
-
-
-
r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
-
r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
-
r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
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-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
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-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
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-
-
r
acetaldehyde + NADPH + H+
ethanol + NADP+
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-
-
r
acetaldehyde + NADPH + H+
ethanol + NADP+
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-
-
r
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
-
-
-
r
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
-
-
-
r
furfural + NADH + H+
furfuryl alcohol + NAD+
-
-
-
r
furfural + NADH + H+
furfuryl alcohol + NAD+
-
-
-
r
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NADH
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-
NADH
-
less effective cofactor
NADH
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less effective cofactor
NADH
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less effective cofactor
NADH
-
less effective cofactor
NADP+
-
-
NADPH
-
-
NADPH
-
preferred cofactor
NADPH
-
preferred cofactor
NADPH
-
preferred cofactor
NADPH
-
preferred cofactor
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Ca2+
slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate
Mg2+
slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate
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2-methylbutanal
-
presence of NADPH, Ki: 2.74 mM, presence of NADH, Ki: 4.61 mM
3-Methylbutanal
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presence of NADPH, Ki: 7.14 mM, presence of NADH, Ki: 253 mM
Butanal
-
presence of NADPH, Ki: 16.6 mM
dithiothreitol
-
35% inhibition at 5 mM
glutathione
-
24% inhibition at 5 mM
Heptanal
-
presence of NADPH, Ki: 0.88 mM, presence of NADH, Ki: 1.17 mM
hexanal
-
presence of NADPH, Ki: 0.79 mM, presence of NADH, Ki: 2.8 mM
NADP+
-
complete inhibition at a 6.7fold excess of NADP+ in a reduction assay with 0.15 mM NADH
pentanal
-
presence of NADPH, Ki: 3.9 mM, presence of NADH, Ki: 13.9 mM
propanal
-
presence of NADPH, Ki: 46.6 mM
quercetin
-
78% inhibition at 0.1 mM
sodium valporate
-
5% inhibition at 1 mM
2-mercaptoethanol
-
6% inhibition at 10 mM
2-mercaptoethanol
inhibition level depends on the substrate used, about 40% inhibition at 10 mM
Ca2+
-
9% inhibition at 0.1 mM
Ca2+
slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate
KCl
-
16% inhibition at 0.2 M
KCl
-
5-6fold decreasing activity at 0.2 M for NADH-dependent activity
Mg2+
-
6% inhibition at 0.1 mM
Mg2+
slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate
NaCl
-
19% inhibition at 0.2 M
NaCl
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5-6fold decreasing activity at 0.2 M for NADH-dependent activity
Zn2+
-
28% inhibition at 0.1 mM
additional information
the strength of inhibition by metal ions depends on the substrate used, overview
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additional information
-
the strength of inhibition by metal ions depends on the substrate used, overview
-
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KCl
-
5-6fold increasing activity for NADPH-dependent activity at 0.2 M
NaCl
-
5-6fold increasing activity for NADPH-dependent activity at 0.2 M
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1.85 - 17.7
2-methylbutanal
0.12 - 11.1
3-Methylbutanal
97.37
furfural
pH 7.0, 30°C
16.11
glycolaldehyde
pH 7.0, 30°C
1.22
Hexanol
-
presence of NADP+
1.69
trans-2-hexenol
-
presence of NADP+
1.85
2-methylbutanal
-
presence of NADPH
17.7
2-methylbutanal
-
presence of NADH
0.12
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
0.14
3-Methylbutanal
wild-type, pH 7.5, 30°C
0.18
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
0.2
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
0.21
3-Methylbutanal
-
presence of NADPH
0.23
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
0.67
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
1.89
3-Methylbutanal
-
presence of NADH
4.1
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
11.1
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
0.74
acetaldehyde
pH 7.0, 30°C
158
acetaldehyde
-
presence of NADPH
2.76
Butanal
-
presence of NADPH
23.1
Butanal
-
presence of NADH
0.27
Heptanal
-
presence of NADPH
4.25
Heptanal
-
presence of NADH
0.18
hexanal
-
presence of NADPH
0.83
hexanal
-
presence of NADH
0.16
pentanal
-
presence of NADPH
3.01
pentanal
-
presence of NADH
27
propanal
-
presence of NADH
38.9
propanal
-
presence of NADPH
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92.3 - 113
2-methylbutanal
1.4 - 91.8
3-Methylbutanal
5.6 - 313.14
acetaldehyde
36.9
furfural
pH 7.0, 30°C
15.44
glycolaldehyde
pH 7.0, 30°C
2.55
Hexanol
-
in the presence of NADP+
14
trans-2-hexenol
-
in the presence of NADP+
92.3
2-methylbutanal
-
presence of NADH
113
2-methylbutanal
-
presence of NADPH
1.4
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
5.9
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
9.3
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
15.5
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
23.2
3-Methylbutanal
wild-type, pH 7.5, 30°C
38.9
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
52.6
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
62.4
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
74.9
3-Methylbutanal
-
presence of NADPH
91.8
3-Methylbutanal
-
presence of NADH
5.6
acetaldehyde
-
in the presence of NADPH
313.14
acetaldehyde
pH 7.0, 30°C
47.3
Butanal
-
presence of NADH
57
Butanal
-
presence of NADPH
72.9
Heptanal
-
presence of NADPH
101
Heptanal
-
presence of NADH
50.1
hexanal
-
presence of NADH
71.1
hexanal
-
presence of NADPH
56.6
pentanal
-
presence of NADPH
81.6
pentanal
-
presence of NADH
55
propanal
-
presence of NADPH
84
propanal
-
presence of NADH
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0.53 - 342.7
3-Methylbutanal
423.16
acetaldehyde
pH 7.0, 30°C
0.39
furfural
pH 7.0, 30°C
0.96
glycolaldehyde
pH 7.0, 30°C
0.53
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
2.1
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
2.3
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
126.3
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
161
3-Methylbutanal
wild-type, pH 7.5, 30°C
166.6
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
261.5
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
342.7
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
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0.74
substrate 3-methylbutanal, pH 7.0, 30°C
1.12
substrate benzaldehyde, pH 7.0, 30°C
1.74
substrate 5-hydroxymethylfurfural, pH 7.0, 30°C
190.86
substrate acetaldegyde, pH 7.0, 30°C
5.05
substrate furfural, pH 7.0, 30°C
61.6
-
in the presence of NADPH
9.64
substrate glycolaldehyde, pH 7.0, 30°C
93.9
-
in the presence of NADH
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5 - 6
optimum pH of Ymr152wp is acidic at pH 5.0-6.0, but this enzyme is more stable in alkaline conditions at pH 8.0, relative activity of Ymr152wp drops quickly under alkaline conditions from pH 7.0 to pH 9.0. The highest enzyme activity of Ymr152wp is observed at pH 5.5 with furfural as substrate, 15% of maximal activity at pH 9.0, 40% at pH 6.5. The optimum pH for reduction of glycolaldehyde is pH 6.0.showing more than 80% of its maximal enzyme activity at pH 4.5-8.5
6 - 7
-
NADH-dependent activity, highest activity at low ionic strength
8.5
-
NADPH-dependent activity, highest activity at high ionic strength
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20 - 50
70% of maximal activity at 20°C, maximal activity at 25-30°C, low activity at 60°C
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brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
brewer's yeast
-
-
brenda
cf. EC 1.1.1.283
UniProt
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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-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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-
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
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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
evolution
phylogenetic analysis indicates that Ymr152wp and selected proteins similar to Ymr152wp are classified into the MDR family, which is close to the QOR subfamily and the LTD subfamily, but is far from the zinc-containing subfamilies of the ADH subfamily, the CADH subfamily, and the YADH subfamily in the genetic tree
evolution
-
phylogenetic analysis indicates that Ymr152wp and selected proteins similar to Ymr152wp are classified into the MDR family, which is close to the QOR subfamily and the LTD subfamily, but is far from the zinc-containing subfamilies of the ADH subfamily, the CADH subfamily, and the YADH subfamily in the genetic tree
-
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GRE2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
342
0
38170
Swiss-Prot
other Location (Reliability: 3 )
YIM1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
365
0
41637
Swiss-Prot
other Location (Reliability: 1 )
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monomer
-
1 * 37000, SDS-PAGE
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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
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F132A
about 200% of wild-type activity
F85A
less than 0.5% of wild-type activity
L169L
complete loss of activity
S127A
complete loss of activity
V162A
about 150% of wild-type activity
V198A
about 1.5% of wild-type activity
Y128A
about 1.5% of wild-type activity
Y128F
activity similar to wild-type
Y165A
complete loss of activity
Y165F
complete loss of activity
Y198F
about 75% of wild-type activity
additional information
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creation of a knockout mutant that forms large, invasive filaments
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8
optimum pH of Ymr152wp is acidic at pH 5.0-6.0, but this enzyme is more stable in alkaline conditions at pH 8.0
763285
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60
Ymr152wp completely loses its catalytic activities for reduction of furfural after incubation at 60°C for 15 min, and for reduction of acetaldehyde and glycolaldehyde after incubation at 60°C for 30 min
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to homogeneity, chromatography techniques
-
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expression in Escherichia coli
gene YMR152W, sequence comparison and phylogenetic analysis
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nutrition
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essential in removal of the worthy off-flavours in beer during fermentation
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Perpete, P.; Collin, S.
Contribution of 3-methylthiopropionaldehyde to the worty flavor of alcohol-free beers
J. Agric. Food Chem.
47
2374-2378
1999
Saccharomyces cerevisiae, [Candida] boidinii, Saccharomyces bayanus, Saccharomycodes ludwigii
brenda
Van Nedervelde, L.; Verlingen, V.; Philipp, D.; Debourg, A.
Purificationa nd characterization of yeast 3-methyl butanal reductases involved in the removal of wort carbonyls during fermentation
Proc. Congr. Eur. Brew. Conv.
26
447-454
1997
Saccharomyces cerevisiae
-
brenda
Van Iersel, M.F.; Eppink, M.H.; van Berkel, W.J.; Rombouts, F.M.; Abee, T.
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae
Appl. Environ. Microbiol.
63
4079-4082
1997
Saccharomyces cerevisiae
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
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), Saccharomyces cerevisiae
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)
brenda
Warringer, J.; Blomberg, A.
Involvement of yeast YOL151W/GRE2 in ergosterol metabolism
Yeast
23
389-398
2006
Saccharomyces cerevisiae (Q12068), Saccharomyces cerevisiae
brenda
Ouyang, Y.; Li, Q.; Kuang, X.; Wang, H.; Wu, J.; Ayepa, E.; Chen, H.; Abrha, G.; Zhang, Z.; Li, X.; Ma, M.
YMR152W from Saccharomyces cerevisiae encoding a novel aldehyde reductase for detoxification of aldehydes derived from lignocellulosic biomass
J. Biosci. Bioeng.
131
39-46
2021
Saccharomyces cerevisiae (P28625), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P28625)
brenda
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