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Information on EC 3.1.2.20 - acyl-CoA hydrolase and Organism(s) Escherichia coli and UniProt Accession P0A8Z0

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.20 acyl-CoA hydrolase
IUBMB Comments
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0A8Z0
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
acyl-coa hydrolase, them2, type ii thioesterase, them1, acot13, thioesterase superfamily member 2, acot11, te ii, them4, hthem2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACH1
-
-
-
0
ACH2
-
-
-
0
ACT
-
-
-
0
acyl CoA hydrolase
-
-
-
0
acyl coenzyme A hydrolase
-
-
-
0
acyl coenzyme A thioesterase
-
-
-
0
acyl-CoA hydrolase
276386
-
acyl-CoA thioesterase
-
-
-
0
brain acyl-CoA hydrolase
-
-
-
0
fatty acyl thioesterase I
-
-
-
0
HIV-Nef associated acyl coA thioesterase
-
-
-
0
hydrolase, acyl coenzyme A
-
-
-
0
hydrolase, palmitoyl coenzyme A
-
-
-
0
LACH1
-
-
-
0
LACH2
-
-
-
0
long chain acyl-CoA hydrolase
-
-
-
0
long chain acyl-CoA thioesterase
-
-
-
0
long chain fatty-acyl-CoA hydrolase
-
-
-
0
long chain fatty-acyl-CoA thioesterase
-
-
-
0
mitochondrial acyl-CoA thioesterase
-
-
-
0
palmitoyl coenzyme A hydrolase
-
-
-
0
palmitoyl thioesterase
-
-
-
0
palmitoyl-CoA deacylase
-
-
-
0
palmitoyl-CoA hydrolase
-
-
-
0
palmityl coenzyme A deacylase
-
-
-
0
palmityl thioesterase
-
-
-
0
palmityl thioesterase I
-
-
-
0
palmityl thioesterase II
-
-
-
0
TE
-
-
-
0
TE-II
-
-
-
0
thioesterase
276386
-
thioesterase B
-
-
-
0
thioesterase II
-
-
-
0
thioesterase III
295975
-
very long chain acyl-CoA thioesterase
-
-
-
0
ybaW protein
295975
-
YciA
276386
-
ZAP128
-
-
-
0
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
hydrolysis of thioester
-
-
-
0
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA hydrolase
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
CAS REGISTRY NUMBER
COMMENTARY hide
37270-64-7
EC 3.1.2.2
9025-87-0
EC 3.1.2.20
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
beta-methylcrotonyl-CoA + H2O
CoA + beta-methylcrotonate
show the reaction diagram
-
-
-
?
isobutyryl-CoA + H2O
CoA + isobutyrate
show the reaction diagram
-
-
-
?
lauroyl-CoA + H2O
CoA + laurate
show the reaction diagram
-
-
-
?
n-butyryl-CoA + H2O
CoA + n-butyrate
show the reaction diagram
-
-
-
?
n-butyryl-pantetheine phosphate + H2O
?
show the reaction diagram
-
-
-
?
n-decanoyl-CoA + H2O
CoA + n-decanoate
show the reaction diagram
-
-
-
?
oleoyl-CoA + H2O
CoA + oleate
show the reaction diagram
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
-
-
-
?
phenylacetyl-CoA + H2O
CoA + phenylacetate
show the reaction diagram
-
-
-
?
3,5-cis-dodecadienoyl-CoA + H2O
CoA + 3,5-cis-dodecadienoic acid
show the reaction diagram
-
-
-
?
3,5-cis-tetradecadienoyl-CoA + H2O
CoA + 3,5-cis-tetradecadienoic acid
show the reaction diagram
-
-
-
?
3-hydroxytetradecanoyl-CoA + H2O
CoA + 3-hydroxytetradecanoate
show the reaction diagram
-
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
arachidoyl-CoA + H2O
CoA + arachidate
show the reaction diagram
-
-
-
?
decanoyl-CoA + H2O
CoA + decanoate
show the reaction diagram
dodecanoyl-CoA + H2O
CoA + dodecanoate
show the reaction diagram
-
i.e. lauroyl-CoA
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
show the reaction diagram
hexanoyl-CoA + H2O
CoA + hexanoate
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + H2O
CoA + laurate
show the reaction diagram
-
-
-
?
myristoyl-CoA + H2O
CoA + myristate
show the reaction diagram
-
-
-
?
octadecanoyl-CoA + H2O
CoA + octadecanoate
show the reaction diagram
oleoyl pantetheine + H2O
oleate + pantetheine
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + H2O
CoA + oleate
show the reaction diagram
-
-
-
-
?
oleyl-[acyl-carrier protein] + H2O
oleate + acyl-carrier protein
show the reaction diagram
-
-
-
-
?
palmitoleoyl-CoA + H2O
CoA + palmitoleoate
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
show the reaction diagram
-
i.e. myristoyl-CoA
-
-
?
vaccenoyl-CoA + H2O
CoA + vaccenoate
show the reaction diagram
-
cis-isomer
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-Hydroxybenzoyl-CoA + H2O
4-Hydroxybenzoate + CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyphenacyl-CoA
-
CoA
strong feedback inhibitor, product inhibition
2,4-dinitrofluorobenzene
-
inhibits very slowly
diethyldicarbonate
hydroxylamine reverses
diisopropylfluorophosphate
iodoacetamide
-
-
methylene blue
-
photooxidation
PMSF
-
less effective than DFP, produces a 27% loss of activity under similar conditions
additional information
no inhibition by iodoacetate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
4-hydroxybenzoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.167
acetyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.29
beta-methylcrotonyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.015
isobutyryl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.02
lauroyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.068
n-butyryl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.8
n-butyryl-pantetheine phosphate
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.013
n-decanoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.011
oleoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
33
palmitoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.016
phenylacetyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.0108
3,5-cis-dodecadienoyl-CoA
-
0.003
3,5-cis-tetradecadienoyl-CoA
-
0.0058
3-hydroxytetradecanoyl-CoA
-
0.00013 - 0.006
fatty-acyl-CoA thioester
-
-
0.013
lauroyl-CoA
-
0.0063
myristoyl-CoA
-
0.006
palmitoyl-CoA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0062
4-hydroxybenzoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.55
acetyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.1
beta-methylcrotonyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
9.5
isobutyryl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
9.6
lauroyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
6.7
n-butyryl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
0.082
n-butyryl-pantetheine phosphate
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
17
n-decanoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
13
oleoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
3.7
palmitoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
9.4
phenylacetyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
21.6
3,5-cis-dodecadienoyl-CoA
-
2 - 3.7
3,5-cis-tetradecadienoyl-CoA
-
10.7
3-hydroxytetradecanoyl-CoA
-
1.6
lauroyl-CoA
-
6.2
myristoyl-CoA
-
10.2
palmitoyl-CoA
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2000
3,5-cis-dodecadienoyl-CoA
-
7900
3,5-cis-tetradecadienoyl-CoA
-
1800
3-hydroxytetradecanoyl-CoA
-
100
lauroyl-CoA
-
1000
myristoyl-CoA
-
1700
palmitoyl-CoA
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0054
hexyl-CoA
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
101.3
with 3,5-cis-tetradecadienoyl-CoA
26.4
with myristoyl-CoA
43.5
with palmitoyl-CoA
45.5
with 3-hydroxytetradecanoyl-CoA
6.9
with lauroyl-CoA
92.3
with 3,5-cis-dodecadienoyl-CoA
93.8
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
-
-
7 - 9.8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15160
His-tagged YciA protein, determined by electrospray ionization mass spectrometry
122000
-
gel filtration, thioesterase I
123000
recombinant enzyme, native PAGE
15000
4 * 15000, crystal structure analysis, SDS-PAGE
20000
20000 - 23000
-
gel filtration
30000
-
4 * 30000, SDS-PAGE
90000
-
gel filtration, palmityl thioesterase II
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
YciA determined by using equilibrium sedimentation techniques
homotetramer
4 * 15000, crystal structure analysis, SDS-PAGE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, protein solution: 10 mg/ml, 5 mM NH4OH, 2 mM DTT, over equal volume of reservoir solution: 1-2 M NaCl, 0.1 M sodium formate, pH 6.0, 2 mM N,N-dimethyl-dodecylamine oxide-LDAO, few days, X-ray structure determination and analysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
646120
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
YciA tends to precipitate at high concentrations
bovine serum albumin stabilizes
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C over 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cells are harvested by centrifugation and suspended in lysis buffer, passed through a French press and centrifuged. The supernatant is loaded onto a Ni-NTA agarose column. The column is washed with a buffer containing 50 mM NaH2PO4, 300 mM NaCl, 50 mM imidazole and 1 mM dithiothreitol, and then the YciA is eluted with an imidazole gradient up to 250 mM imidazole. The pooled and concentrated fractions are chromatographed on a size exclusion column using a buffer containing 50 mM NaH2PO4, 50 mM NaCl, 10 mM imidazole and 1 mM dithiothreitol.
20fold, palmityl thioesterase II, palmityl thioesterase I
-
ion exchange chromatography (DEAE-cellulose), hydroxylapatite chromatography, hydrophobic interaction chromatography, recombinant protein: immobilized metal ion affinity chromatography (Ni2+), ion exchange chromatography (DEAE-cellulose), hydrophobic interaction chromatography
native wild-type: 8000fold to homogeneity
recombinant wild-type: 4fold to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene encoding YciA is amplified by PCR and expressed in Escherichia coli strain BL21 (DE3)
gene tes B, DNA sequence determination and analysis, no sequence similarity between Escherichia coli thioesterase II and the two types of mammalian thioesterases, i.e. the chain-terminating enzymes of de novo fatty acid synthesis
gene tesB, overexpression in the Escherichia coli host strain
heterologous expression of tesB in Pseudomonas putida GPp104
-
His-tagged version expressed in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barnes jr., E.M.; Wakil, S.J.
Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase
J. Biol. Chem.
243
2955-2962
1968
Columba sp., Escherichia coli
Manually annotated by BRENDA team
Bonner, W.M.; Bloch, K.
Purification and properties of fatty acyl thioesterase I from Escherichia coli
J. Biol. Chem.
247
3123-3133
1972
Escherichia coli
Manually annotated by BRENDA team
Barnes jr., E.M.
Long-chain fatty acyl thioesterases I and II from Escherichia coli
Methods Enzymol.
35
102-109
1975
Escherichia coli
Manually annotated by BRENDA team
Poupon, V.; Begue, B.; Gagnon, J.; Dautry-Varsat, A.; Cerf-Bensussan, N.; Benmerah, A.
Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase
J. Biol. Chem.
274
19188-19194
1999
Arabidopsis thaliana, Bacillus subtilis, Caenorhabditis elegans, Oryctolagus cuniculus, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Rattus norvegicus, Mus musculus (Q9R0X4)
Manually annotated by BRENDA team
Naggert, J.; Narasimhan, M.L.; DeVeaux, L.; Cho, H.; Randhawa, Z.I.; Cronan, J.E.; Green, B.N.; Smith, S.
Cloning, sequencing, and characterization of Escherichia coli thioesterase II
J. Biol. Chem.
266
11044-11050
1991
Escherichia coli (P0AGG2)
Manually annotated by BRENDA team
Swenson, L.; Green, R.; Smith, S.; Derewenda, Z.S.
Crystallization of thioesterase II from Escherichia coli
J. Mol. Biol.
236
660-662
1994
Escherichia coli (P0AGG2)
Manually annotated by BRENDA team
Zheng, Z.; Gong, Q.; Liu, T.; Deng, Y.; Chen, J.C.; Chen, G.Q.
Thioesterase II of Escherichia coli plays an important role in 3-hydroxydecanoic acid production
Appl. Environ. Microbiol.
70
3807-3813
2004
Escherichia coli
Manually annotated by BRENDA team
Zhuang, Z.; Song, F.; Zhao, H.; Li, L.; Cao, J.; Eisenstein, E.; Herzberg, O.; Dunaway-Mariano, D.
Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA
Biochemistry
47
2789-2796
2008
Escherichia coli (P0A8Z0), Haemophilus influenzae (P44886)
Manually annotated by BRENDA team
Nie, L.; Ren, Y.; Schulz, H.
Identification and characterization of Escherichia coli thioesterase III that functions in fatty acid beta-oxidation
Biochemistry
47
7744-7751
2008
Escherichia coli (P77712), Escherichia coli
Manually annotated by BRENDA team
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