Information on EC 5.3.3.14 - trans-2-decenoyl-[acyl-carrier protein] isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.3.14
-
RECOMMENDED NAME
GeneOntology No.
trans-2-decenoyl-[acyl-carrier protein] isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5Z)-dodec-5-enoate biosynthesis I
-
-
(5Z)-dodec-5-enoate biosynthesis II
-
-
Fatty acid biosynthesis
-
-
mycolate biosynthesis
-
-
oleate biosynthesis IV (anaerobic)
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lipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
decenoyl-[acyl-carrier protein] Delta2-trans-Delta3-cis-isomerase
While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-80-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cis-3-decenoyl-N-acetylcysteamine
trans-2-decenoyl-N-acetylcysteamine
show the reaction diagram
-
-
-
-
r
cis-beta,gamma-decenoyl-N-acetylcysteamine
?
show the reaction diagram
-
-
-
-
?
trans-2-decenoyl-(acyl-carrier protein)
cis-3-decenoyl-(acyl-carrier protein)
show the reaction diagram
-
enzyme is equally active with acyl carrier protein derived from Escherichia coli, spinach or a protein A:acyl carrier protein fusion protein. With acyl carrier protein derived from Escherichia coli or from spinach, equilibrium results in equal amounts of trans-3- or cis-2-decenoyl-(acyl-carrier-protein), regardless of the initial substrate. With the fusion protein, yield is about 17% cis-3- and 49% trans-2-decenoyl-(acyl-carrier-protein)
-
-
r
trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
show the reaction diagram
trans-2-octenoyl-N-acetylcysteamine
cis-3-octenoyl-N-acetylcysteamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-decynoyl-N-acetylcysteamine
3-dodecynoyl-N-acetylcysteamine
-
-
3-nonynoyl-N-acetylcysteamine
-
noncompetitive
3-octynoyl-N-acetylcysteamine
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24% inhibition at 0.005 mM
3-undecynoyl-N-acetylcysteamine
-
-
p-chloromercuribenzoate
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0.5 mM, 35% inhibition
additional information
-
not inhibitory: iodoacetic acid, chloroacetic acid, iodoacetamide, N-ethylmaleimide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
cis-beta,gamma-Decenoyl-N-acetylcysteamine
-
pH 7.0
additional information
additional information
-
Km-value gradually decreases with decreasing pH-value
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
cis-3-decenoyl-N-acetylcysteamine
Escherichia coli
-
pH 9.0, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013
3-decynoyl-N-acetylcysteamine
-
pH 7.0, 30C, isomerase acitivity
0.00075
3-dodecynoyl-N-acetylcysteamine
-
pH 7.0, 30C, isomerase acitivity
0.00023
3-nonynoyl-N-acetylcysteamine
-
pH 7.0, 30C, isomerase acitivity
0.00019
3-undecynoyl-N-acetylcysteamine
-
pH 7.0, 30C, isomerase acitivity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000087
-
pH 7.0
additional information
-
direct assay for enzyme activity based on substrate analogues
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.95
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 10.2
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more than 50% of activity maximum within this range
PDB
SCOP
CATH
ORGANISM
UNIPROT
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
Human immunodeficiency virus type 1 group M subtype D
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
2 * 18000, SDS-PAGE
18800
x * 18800, calculated
27500
-
sucrose density sedimentation
28000
-
gel filtration
31000
-
4 * 31000, SDS-PAGE
36000
-
gel filtration
129000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 18800, calculated
tetramer
-
4 * 31000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free enzyme and modified by inhibitor 3-decynoyl-N-acteylcysteamine
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
simplified purification protocol
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme insertion mutant, no production of unsaturated fatty acids by mutant strain. Strain is extremely sensitive to low pH-values and exhibits reduced glycolyic capability and altered membrane composition, resulting in higher impermeability to protons
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