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Information on EC 1.1.1.265 - 3-methylbutanal reductase
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1.1.1.265 3-methylbutanal reductaseIUBMB 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.
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Word Map
- 1.1.1.265
-
enantioselectivity
- ketoreductase
- furfural
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lignocellulosic
- 5-hydroxymethylfurfural
- glycolaldehyde
- butanoate
- benzaldehyde
- l-carnitine
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aldo-keto
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sporobolomyces
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spycatcher
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desalting
- salmonicolor
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spytag
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1-dehydrogenase
- nutrition
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
yol151w, gre2p, ymr152wp, ymr152w, 3-methylbutanal reductase, isovaleraldehyde reductase, branched-chain alcohol dehydrogenase, gre2 gene product, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-methylbutyraldehyde reductase
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aldehyde reductase
isoamylaldehyde reductase
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isopentanal reductase
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isovaleral reductase
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isovaleraldehyde reductase
protein YIM1
YIM1
YMR152W
Ymr152wp
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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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
214265-44-8
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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
2,3-pentanedione + NAD(P)H
? + NAD(P)+
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very low activity
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?
3-methylbutanal + NAD(P)H + H+
3-methylbutanol + NAD(P)+
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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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?
5-hydroxymethylfurfural + NADH + H+
2,5-dihydroxymethylfurane + NAD+
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r
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
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
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
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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?
3-methylbutanal + NADPH + H+
3-methylbutanol + NADP+
low activity
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r
acetaldehyde + NADH + H+
ethanol + NAD+
best substrate
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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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?
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
low activity
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r
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
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r
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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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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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
5-hydroxymethylfurfural + NADH + H+
2,5-dihydroxymethylfurane + NAD+
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r
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
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
benzaldehyde + NADPH + H+
benzylalcohol + NADP+
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r
furfural + NADH + H+
furfuryl alcohol + NAD+
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
2-mercaptoethanol
inhibition level depends on the substrate used, about 40% inhibition at 10 mM
Ca2+
slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate
KCl
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5-6fold decreasing activity at 0.2 M for NADH-dependent activity
Mg2+
slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate
NaCl
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5-6fold decreasing activity at 0.2 M for NADH-dependent activity
additional information
the strength of inhibition by metal ions depends on the substrate used, overview
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additional information
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the strength of inhibition by metal ions depends on the substrate used, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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