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Information on EC 1.3.1.27 - 2-hexadecenal reductase and Organism(s) Homo sapiens and UniProt Accession Q08257

for references in articles please use BRENDA:EC1.3.1.27
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IUBMB Comments
Specific for long chain 2-trans- and 2-cis-alkenals, with chain length optimum around 14 to 16 carbon atoms.
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This record set is specific for:
Homo sapiens
UNIPROT: Q08257
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-alkenal reductase, zmaer, nadph-dependent 2-alkenal reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
zeta-Crystallin
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2-alkenal reductase
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-
-
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hexadecanal: NADP+ oxidoreductase
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reductase, 2-alkenal
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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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
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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-nonenal + NADPH + H+
nonanal + NADP+
show the reaction diagram
-
-
-
ir
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
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-
-
?
4-hydroxy-2-nonenal + NADPH + H+
4-hydroxynonanal + NADP+
show the reaction diagram
-
-
-
?
additional information
?
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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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48
2-nonenal
wild-type, pH 7.5, temperature not specified in the publication
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.113
2-nonenal
wild-type, pH 7.5, temperature not specified in the publication
0.167
3-buten-2-one
wild-type, pH 7.5, temperature not specified in the publication
1.33
4-hydroxy-2-hexenal
wild-type, pH 7.5, temperature not specified in the publication
1.15
4-hydroxy-2-nonenal
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
wild-type, pH 7.5, temperature not specified in the publication
4.8
3-buten-2-one
wild-type, pH 7.5, temperature not specified in the publication
0.02 - 10.2
4-hydroxy-2-hexenal
2.1
4-hydroxy-2-nonenal
wild-type, pH 7.5, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
QOR_HUMAN
329
0
35207
Swiss-Prot
-
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
PROTEIN VARIANTS
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Porte, S.; Moeini, A.; Reche, I.; Shafqat, N.; Oppermann, U.; Farres, J.; Pares, X.
Kinetic and structural evidence of the alkenal/one reductase specificity of human zeta-crystallin
Cell. Mol. Life Sci.
68
1065-1077
2011
Homo sapiens (Q08257)
Manually annotated by BRENDA team