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Information on EC 5.3.3.14 - trans-2-decenoyl-[acyl-carrier protein] isomerase and Organism(s) Escherichia coli and UniProt Accession P0A6Q3

for references in articles please use BRENDA:EC5.3.3.14
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IUBMB Comments
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 . 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.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A6Q3
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
FabM, more
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 SOURCE
PATHWAYS
-
-, -, -, -
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
-
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
-
-
-
-
r
additional information
?
-
-
enzyme activity depends more on acyl chain length than acyl carrier protein structure or origin
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-decynoyl-N-acetylcysteamine
3-dodecynoyl-N-acetylcysteamine
-
-
3-nonynoyl-N-acetylcysteamine
-
noncompetitive
3-octynoyl-N-acetylcysteamine
-
24% inhibition at 0.005 mM
3-undecynoyl-N-acetylcysteamine
-
-
p-chloromercuribenzoate
-
0.5 mM, 35% inhibition
additional information
-
not inhibitory: iodoacetic acid, chloroacetic acid, iodoacetamide, N-ethylmaleimide
-
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
-
pH 9.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013
3-decynoyl-N-acetylcysteamine
-
pH 7.0, 30°C, isomerase acitivity
0.00075
3-dodecynoyl-N-acetylcysteamine
-
pH 7.0, 30°C, isomerase acitivity
0.00023
3-nonynoyl-N-acetylcysteamine
-
pH 7.0, 30°C, isomerase acitivity
0.00019
3-undecynoyl-N-acetylcysteamine
-
pH 7.0, 30°C, isomerase acitivity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.95
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 10.2
-
more than 50% of activity maximum within this range
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
Swissprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18800
x * 18800, calculated
18000
-
2 * 18000, SDS-PAGE
27500
-
sucrose density sedimentation
28000
-
gel filtration
36000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 18800, calculated
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and modified by inhibitor 3-decynoyl-N-acteylcysteamine
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
simplified purification protocol
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kass, L.R.; Brock, D.J.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
242
4418-4431
1967
Escherichia coli
Manually annotated by BRENDA team
Helmkamp, G.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase. Studies on molecular structure and active site
J. Biol. Chem.
244
6014-6022
1969
Escherichia coli
Manually annotated by BRENDA team
Helmkamp, G.; Rando, R.R.; Brock, D.J.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
243
3229-3231
1968
Escherichia coli
Manually annotated by BRENDA team
Endo, K.; Helmkamp, G.M.; Bloch, K.
Mode of inhibition of beta-hydroxydecanoyl thioester dehydrase by 3-decynoyl-N-acetylcysteamine
J. Biol. Chem.
245
4293-4296
1970
Escherichia coli
Manually annotated by BRENDA team
Cronan, J.E.; Li, W.B.; Coleman, R.; Narasimhan, M.; De Mendoza, D.; Schwab, J.M.
Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
263
4641-4646
1988
Escherichia coli (P0A6Q3)
Manually annotated by BRENDA team
Guerra, D.J.; Browse, J.A.
Escherichia coli beta-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin
Arch. Biochem. Biophys.
280
336-345
1990
Escherichia coli
Manually annotated by BRENDA team
Rando, R.R.; Bloch, K.
Mechanism of action of beta-hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
243
5627-5634
1968
Escherichia coli
Manually annotated by BRENDA team
Leesong, M.; Henderson, B.S.; Gillig, J.R.; Schwab, J.M.; Smith, J.L.
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site
Structure
4
253-264
1996
Escherichia coli
Manually annotated by BRENDA team