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Information on EC 1.1.1.265 - 3-methylbutanal reductase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12068
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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
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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 taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
yol151w, gre2p, ymr152wp, ymr152w, 3-methylbutanal reductase, isovaleraldehyde reductase, branched-chain alcohol dehydrogenase, gre2 gene product, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-methylbutyraldehyde reductase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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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.
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
3-methylbutanal + NAD(P)H + H+
3-methylbutanol + NAD(P)+
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r
2,3-pentanedione + NAD(P)H
? + NAD(P)+
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very low activity
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?
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
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
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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?
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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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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-
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
70% of maximal activity at 20°C, maximal activity at 25-30°C, low activity at 60°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
creation of a knockout mutant that forms large, invasive filaments
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
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essential in removal of the worthy off-flavours in beer during fermentation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 bayanus, Saccharomyces cerevisiae, Saccharomycodes ludwigii, [Candida] boidinii
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
-
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
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
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
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)
Warringer, J.; Blomberg, A.
Involvement of yeast YOL151W/GRE2 in ergosterol metabolism
Yeast
23
389-398
2006
Saccharomyces cerevisiae (Q12068), Saccharomyces cerevisiae
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)
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