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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
3-methylbutyraldehyde reductase, bcADH, branched-chain alcohol dehydrogenase, Gre2, GRE2 gene product, Gre2p, isoamylaldehyde reductase, isopentanal reductase, isovaleral reductase, isovaleraldehyde reductase,
more
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3-methylbutyraldehyde reductase
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branched-chain alcohol dehydrogenase
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isoamylaldehyde reductase
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isopentanal reductase
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isovaleral reductase
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isovaleraldehyde reductase
additional information
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enzyme displays also NADPH dependent methylglyoxal reductase activity (EC 1.1.1.283)
isovaleraldehyde reductase
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isovaleraldehyde reductase
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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)+
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very low activity
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?
2-methylbutanal + NAD(P)H
2-methylbutanol + NAD(P)+
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
3-methylbutanal + NAD(P)H + H+
3-methylbutanol + NAD(P)+
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r
3-methylbutanal + NADH + H+
3-methylbutanol + NAD+
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r
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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?
acetaldehyde + NADPH + H+
ethanol + NADP+
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
butanal + NAD(P)H + H+
butanol + NAD(P)+
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r
diacetyl + NAD(P)H
? + NAD(P)+
furaldehyde + NAD(P)H
furfuryl alcohol + NAD(P)+
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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?
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
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?
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
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?
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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enzyme displays also NADPH dependent methylglyoxal reductase activity (EC 1.1.1.283)
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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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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 + NADPH + H+
ethanol + NADP+
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r
acetaldehyde + NADPH + H+
ethanol + NADP+
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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
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?
diacetyl + NAD(P)H
? + NAD(P)+
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very low activity
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?
diacetyl + NAD(P)H
? + NAD(P)+
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very low activity
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?
furaldehyde + NAD(P)H
furfuryl alcohol + NAD(P)+
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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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?
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
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3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
acetaldehyde + NADPH + H+
ethanol + NADP+
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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?
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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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
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 + NADPH + H+
ethanol + NADP+
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r
acetaldehyde + NADPH + H+
ethanol + NADP+
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r
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NADH
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NADH
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less effective cofactor
NADH
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less effective cofactor
NADH
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less effective cofactor
NADH
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less effective cofactor
NADPH
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NADPH
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preferred cofactor
NADPH
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preferred cofactor
NADPH
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preferred cofactor
NADPH
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preferred cofactor
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2-mercaptoethanol
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6% inhibition at 10 mM
2-methylbutanal
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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
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presence of NADPH, Ki: 16.6 mM
Ca2+
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9% inhibition at 0.1 mM
dithiothreitol
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35% inhibition at 5 mM
glutathione
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24% inhibition at 5 mM
Heptanal
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presence of NADPH, Ki: 0.88 mM, presence of NADH, Ki: 1.17 mM
hexanal
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presence of NADPH, Ki: 0.79 mM, presence of NADH, Ki: 2.8 mM
Mg2+
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6% inhibition at 0.1 mM
NADP+
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complete inhibition at a 6.7fold excess of NADP+ in a reduction assay with 0.15 mM NADH
pentanal
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presence of NADPH, Ki: 3.9 mM, presence of NADH, Ki: 13.9 mM
propanal
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presence of NADPH, Ki: 46.6 mM
quercetin
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78% inhibition at 0.1 mM
sodium valporate
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5% inhibition at 1 mM
Zn2+
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28% inhibition at 0.1 mM
KCl
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16% inhibition at 0.2 M
KCl
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5-6fold decreasing activity at 0.2 M for NADH-dependent activity
NaCl
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19% inhibition at 0.2 M
NaCl
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5-6fold decreasing activity at 0.2 M for NADH-dependent activity
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KCl
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5-6fold increasing activity for NADPH-dependent activity at 0.2 M
NaCl
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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
158
acetaldehyde
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presence of NADPH
1.22
Hexanol
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presence of NADP+
1.69
trans-2-hexenol
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presence of NADP+
1.85
2-methylbutanal
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presence of NADPH
17.7
2-methylbutanal
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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
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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
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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
2.76
Butanal
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presence of NADPH
23.1
Butanal
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presence of NADH
0.27
Heptanal
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presence of NADPH
4.25
Heptanal
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presence of NADH
0.18
hexanal
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presence of NADPH
0.83
hexanal
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presence of NADH
0.16
pentanal
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presence of NADPH
3.01
pentanal
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presence of NADH
27
propanal
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presence of NADH
38.9
propanal
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presence of NADPH
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92.3 - 113
2-methylbutanal
1.4 - 91.8
3-Methylbutanal
5.6
acetaldehyde
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in the presence of NADPH
2.55
Hexanol
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in the presence of NADP+
14
trans-2-hexenol
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in the presence of NADP+
92.3
2-methylbutanal
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presence of NADH
113
2-methylbutanal
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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
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presence of NADPH
91.8
3-Methylbutanal
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presence of NADH
47.3
Butanal
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presence of NADH
57
Butanal
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presence of NADPH
72.9
Heptanal
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presence of NADPH
101
Heptanal
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presence of NADH
50.1
hexanal
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presence of NADH
71.1
hexanal
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presence of NADPH
56.6
pentanal
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presence of NADPH
81.6
pentanal
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presence of NADH
55
propanal
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presence of NADPH
84
propanal
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presence of NADH
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0.53 - 342.7
3-Methylbutanal
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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61.6
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in the presence of NADPH
93.9
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in the presence of NADH
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6 - 7
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NADH-dependent activity, highest activity at low ionic strength
8.5
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NADPH-dependent activity, highest activity at high ionic strength
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brenda
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brenda
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brenda
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UniProt
brenda
brewer's yeast
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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
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brenda
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brenda
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brenda
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brenda
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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
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GRE2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
342
0
38170
Swiss-Prot
other Location (Reliability: 3 )
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monomer
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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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to homogeneity, chromatography techniques
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expression in Escherichia coli
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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
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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
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