Information on EC 1.3.1.27 - 2-hexadecenal reductase

Word Map on EC 1.3.1.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.27
-
RECOMMENDED NAME
GeneOntology No.
2-hexadecenal reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hexadecanal + NADP+ = 2-trans-hexadecenal + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sphingosine and sphingosine-1-phosphate metabolism
-
-
sphingosine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
hexadecanal:NADP+ DELTA2-oxidoreductase
Specific for long chain 2-trans- and 2-cis-alkenals, with chain length optimum around 14 to 16 carbon atoms.
CAS REGISTRY NUMBER
COMMENTARY hide
52227-95-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
isoform ALH1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-propenal + NAD(P)H
propanal + NAD(P)+
show the reaction diagram
-
-
-
?
1-octen-3-one + NADPH + H+
nonanal + NADP+
show the reaction diagram
-
-
-
-
?
2-nonenal + NADPH + H+
nonanal + NADP+
show the reaction diagram
-
-
-
ir
2-trans,4-trans-hexadienal + NAD(P)H
4-trans-hexenal + NAD(P)+
show the reaction diagram
-
i.e. sorbaldehyde, low reaction rate
-
?
2-trans-hexadecenal + NADPH
hexadecanal + NADP+
show the reaction diagram
2-trans-octadecenal + NADPH
octdecanal + NADP+
show the reaction diagram
-
-
-
r
2-trans-tetradecenal + NADPH
tetradecanal + NADP+
show the reaction diagram
-
-
-
r
3-buten-2-one + NADPH + H+
butan-2-one + NADP+
show the reaction diagram
-
-
-
?
4-hydroxy-2-hexenal + NADPH + H+
4-hydroxyhexadecanal + NADP+
show the reaction diagram
-
-
-
?
4-hydroxy-2-nonenal + NADPH + H+
4-hydroxynonanal + NADP+
show the reaction diagram
-
-
-
?
cis-2-heptenal + NAD(P)H
heptanal + NAD(P)+
show the reaction diagram
-
-
-
?
cis-2-octenal + NAD(P)H
octanal + NAD(P)+
show the reaction diagram
-
best substrate
-
?
trans-2-butenal + NAD(P)H
butanal + NAD(P)+
show the reaction diagram
-
very low reaction rate
-
?
trans-2-cinnamaldehyde + NAD(P)H
cinnamaldehyde + NAD(P)+
show the reaction diagram
-
low reaction rate
-
?
trans-2-decenal + NAD(P)H
decanal + NAD(P)+
show the reaction diagram
trans-2-dodecenal + NAD(P)H
dodecanal + NAD(P)+
show the reaction diagram
-
low reaction rate
-
?
trans-2-heptenal + NAD(P)H
heptanal + NAD(P)+
show the reaction diagram
-
low reaction rate
-
?
trans-2-hexenal + NAD(P)H
hexanal + NAD(P)+
show the reaction diagram
-
low reaction rate
-
?
trans-2-hexenal + NADPH + H+
hexanal + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-nonenal + NAD(P)H
nonanal + NAD(P)H
show the reaction diagram
-
low reaction rate
-
?
trans-2-nonenal + NADPH + H+
nonanal + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-octenal + NAD(P)H
octanal + NAD(P)+
show the reaction diagram
traumatin + NADPH + H+
12-oxododecanoic acid + NADP+
show the reaction diagram
-
i.e. (10E)-12-oxododec-10-enoic acid
-
-
?
additional information
?
-
enzyme additionally catalyzes the reduction of quinones, reaction of EC 1.6.5.5. The enzyme shows a low level of activity with cinnamaldehyde and no activity with 2-cyclohexen-1-one and 15-ketoprostaglandin E2. No activity is detected with nonanal and 2-nonene
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
enzyme is assumed to be a flavoprotein, prosthetic group may be FAD or FMN
NADPH
additional information
-
not FAD-dependent
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
1 mM, complete inhibition
Ca2+
-
50 mM, 40% inhibition
Hg2+
-
1 mM, 86% inhibition
N-ethylmaleimide
-
1 mM, 60% inhibition
p-chloromercuribenzoate
-
1 mM, 90% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
1-octen-3-one
-
pH 6.6
0.025
2-cis-hexadecenal
-
-
0.48
2-nonenal
wild-type, pH 7.5, temperature not specified in the publication
0.013
2-trans-hexadecenal
-
-
0.035
3-buten-2-one
wild-type, pH 7.5, temperature not specified in the publication
0.13 - 3.67
4-hydroxy-2-hexenal
0.55
4-hydroxy-2-nonenal
wild-type, pH 7.5, temperature not specified in the publication
0.005 - 0.06
NADPH
0.01
trans-2-hexenal
-
pH 6.6
0.001
trans-2-nonenal
-
pH 6.6
0.0008
traumatin
-
pH 6.6
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.113
2-nonenal
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
0.167
3-buten-2-one
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
1.33
4-hydroxy-2-hexenal
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
1.15
4-hydroxy-2-nonenal
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
2-nonenal
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
5769
4.8
3-buten-2-one
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
2904
0.02 - 10.2
4-hydroxy-2-hexenal
4640
2.1
4-hydroxy-2-nonenal
Homo sapiens
Q08257
wild-type, pH 7.5, temperature not specified in the publication
1426
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00012
-
enzyme activity in lung
0.00029
-
enzyme activity in kidney
0.00091
-
enzyme activity in heart
0.0017
-
enzyme activity in liver
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
not found in spleen and brain
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
-
gel filtration
45000
-
predominat monomeric form, gel filtration
90000
-
dimeric aggregate, gel filtration
135000
-
trimeric aggregate, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 38000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.85 A resolution. The overall structure displays the typical medium-chain dehydrogenase fold with two domains: the catalytic domain, residues 1-128 and 271-329, and the coenzyme-binding domain, residues 129-270, which are separated by a deep cleft that binds the cofactor NADP+ and the substrate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
labile below pH 4.0
390627
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y53F
substrate-pocket residue, large increase in Km values for all substrates and the cofactor, but mainly towards 3-buten-2-one and propenal with a 30fold increase
Y59F
substrate-pocket residue, almost the same kinetic parameter values as the wild-type enzyme for 2-alkenals
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
-
use of enzyme to improve beer quality by conversion of trans-2-nonenal, the major contributor to the cardboard-like taste of aged beer