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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
-
lignocellulosic
- furfural
-
spycatcher
- salmonicolor
-
sporobolomyces
-
1-dehydrogenase
- l-carnitine
- butanoate
-
desalting
-
aldo-keto
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spytag
- 5-hydroxymethylfurfural
- nutrition
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
isovaleraldehyde reductase
additional information
-
enzyme displays also NADPH dependent methylglyoxal reductase activity (EC 1.1.1.283)
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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
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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)+
-
very low activity
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?
3-methylbutanal + NAD(P)H + H+
3-methylbutanol + NAD(P)+
-
-
-
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)+
-
highest activity
-
?
gluconate + NAD(P)H
D-glucose + NAD(P)+
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very low activity in both reduction and oxidation
-
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
-
?
additional information
?
-
-
enzyme displays also NADPH dependent methylglyoxal reductase activity (EC 1.1.1.283)
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-
?
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
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high activity
-
?
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
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20-50% of the activity with 3-methylbutanal for aromatic aldehydes
-
?
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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?
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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
gluconate + NAD(P)H
D-glucose + NAD(P)+
-
very low activity in both reduction and oxidation
-
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
KCl
-
5-6fold decreasing activity at 0.2 M for NADH-dependent activity
NaCl
-
5-6fold decreasing activity at 0.2 M for NADH-dependent activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
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NADH-dependent activity, highest activity at low ionic strength
8.5
-
NADPH-dependent activity, highest activity at high ionic strength
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GRE2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
342
0
38170
Swiss-Prot
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
creation of a knockout mutant that forms large, invasive filaments
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
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essential in removal of the worthy off-flavours in beer during fermentation
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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 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
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