Information on EC 1.1.1.265 - 3-methylbutanal reductase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.1.1.265
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RECOMMENDED NAME
GeneOntology No.
3-methylbutanal reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+
show the reaction diagram
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 hide
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 hide
214265-44-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
Saccharomyces ludwigii
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-pentanedione + NAD(P)H
? + NAD(P)+
show the reaction diagram
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very low activity
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?
2-methylbutanal + NAD(P)H
2-methylbutanol + NAD(P)+
show the reaction diagram
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r
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
show the reaction diagram
3-methylbutanal + NAD(P)H + H+
3-methylbutanol + NAD(P)+
show the reaction diagram
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r
3-methylthiopropionaldehyde + NADPH + H+
3-methylthiopropanol + NADP+
show the reaction diagram
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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)+
show the reaction diagram
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highest activity
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?
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
show the reaction diagram
butanal + NAD(P)H + H+
butanol + NAD(P)+
show the reaction diagram
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r
diacetyl + NAD(P)H
? + NAD(P)+
show the reaction diagram
furaldehyde + NAD(P)H
furfuryl alcohol + NAD(P)+
show the reaction diagram
gluconate + NAD(P)H
D-glucose + NAD(P)+
show the reaction diagram
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very low activity in both reduction and oxidation
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r
glyceraldehyde + NAD(P)H
glycerol + NAD(P)+
show the reaction diagram
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?
heptanal + NADPH
heptanol + NADP+
show the reaction diagram
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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+
show the reaction diagram
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
show the reaction diagram
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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)+
show the reaction diagram
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low activity
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octanal + NAD(P)H + H+
octanol + NAD(P)+
show the reaction diagram
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?
p-anisaldehyde + NAD(P)H
p-anisalcohol + NAD(P)+
show the reaction diagram
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20-50% of the activity with 3-methylbutanal for aromatic aldehydes
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?
pentanal + NADPH
pentanol + NADP+
show the reaction diagram
propanal + NAD(P)H + H+
propanol + NAD(P)+
show the reaction diagram
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r
trans-2-hexenol + NADP+
trans-2-hexenal + NADPH
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-methylbutanal + NAD(P)H
3-methylbutanol + NAD(P)+
show the reaction diagram
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
gluconate + NAD(P)H
D-glucose + NAD(P)+
show the reaction diagram
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very low activity in both reduction and oxidation
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r
glyceraldehyde + NAD(P)H
glycerol + NAD(P)+
show the reaction diagram
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?
isovaleraldehyde + NADPH + H+
isoamyl alcohol + NADP+
show the reaction diagram
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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 hide
LITERATURE
IMAGE
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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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 hide
LITERATURE
IMAGE
1.85 - 17.7
2-methylbutanal
0.12 - 11.1
3-Methylbutanal
158
acetaldehyde
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presence of NADPH
2.76 - 23.1
Butanal
0.27 - 4.25
Heptanal
0.18 - 0.83
Hexanal
1.22
Hexanol
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presence of NADP+
0.16 - 3.01
pentanal
27 - 38.9
propanal
1.69
trans-2-hexenol
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presence of NADP+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
92.3 - 113
2-methylbutanal
1.4 - 91.8
3-Methylbutanal
5.6
acetaldehyde
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in the presence of NADPH
47.3 - 57
Butanal
72.9 - 101
Heptanal
50.1 - 71.1
Hexanal
2.55
Hexanol
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in the presence of NADP+
56.6 - 81.6
pentanal
55 - 84
propanal
14
trans-2-hexenol
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in the presence of NADP+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53 - 342.7
3-Methylbutanal
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 37000, SDS-PAGE
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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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography techniques
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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essential in removal of the worthy off-flavours in beer during fermentation
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.265)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)