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Information on EC 3.1.2.20 - acyl-CoA hydrolase and Organism(s) Escherichia coli and UniProt Accession P0AGG2
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EC Tree
3.1.2.20 acyl-CoA hydrolaseIUBMB 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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Word Map
- 3.1.2.20
- acyl-coas
- palmitoyl-coa
-
3.1.2.2
-
acyl-coa:cholesterol
- coash
- oleoyl-coa
-
teiis
-
hotdog-fold
-
acots
- arachidonoyl-coa
- degradation
- decanoyl-coa
- biotechnology
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acyl-coa hydrolase, them2, type ii thioesterase, them1, acot11, them4, acot13, thioesterase superfamily member 2, te ii, thioesterase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACH1
-
-
-
-
ACH2
-
-
-
-
ACT
-
-
-
-
acyl CoA hydrolase
-
-
-
-
acyl coenzyme A hydrolase
-
-
-
-
acyl coenzyme A thioesterase
-
-
-
-
acyl-CoA thioesterase
-
-
-
-
brain acyl-CoA hydrolase
-
-
-
-
fatty acyl thioesterase I
-
-
-
-
HIV-Nef associated acyl coA thioesterase
-
-
-
-
hydrolase, acyl coenzyme A
-
-
-
-
hydrolase, palmitoyl coenzyme A
-
-
-
-
LACH1
-
-
-
-
LACH2
-
-
-
-
long chain acyl-CoA hydrolase
-
-
-
-
long chain acyl-CoA thioesterase
-
-
-
-
long chain fatty-acyl-CoA hydrolase
-
-
-
-
long chain fatty-acyl-CoA thioesterase
-
-
-
-
mitochondrial acyl-CoA thioesterase
-
-
-
-
palmitoyl coenzyme A hydrolase
-
-
-
-
palmitoyl thioesterase
-
-
-
-
palmitoyl-CoA deacylase
-
-
-
-
palmitoyl-CoA hydrolase
-
-
-
-
palmityl coenzyme A deacylase
-
-
-
-
palmityl thioesterase
-
-
-
-
palmityl thioesterase I
-
-
-
-
palmityl thioesterase II
-
-
-
-
TE
-
-
-
-
TE-II
-
-
-
-
thioesterase B
-
-
-
-
thioesterase II
-
-
-
-
very long chain acyl-CoA thioesterase
-
-
-
-
ZAP128
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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
37270-64-7
EC 3.1.2.2
9025-87-0
EC 3.1.2.20
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,5-cis-dodecadienoyl-CoA + H2O
CoA + 3,5-cis-dodecadienoic acid
-
-
-
?
3,5-cis-tetradecadienoyl-CoA + H2O
CoA + 3,5-cis-tetradecadienoic acid
-
-
-
?
3-hydroxytetradecanoyl-CoA + H2O
CoA + 3-hydroxytetradecanoate
-
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
-
i.e. myristoyl-CoA
-
-
?
octadecanoyl-CoA + H2O
CoA + octadecanoate
-
i.e. stearoyl-CoA
-
-
?
additional information
?
-
decanoyl pantetheine is no substrate
-
-
?
additional information
?
-
-
the physiological role of thioesterase II in Escherichia coli is to prevent the abnormal accumulation of intracellular acyl-coenzyme A
-
-
?
additional information
?
-
the long, medium, and short chain fatty acyl-CoAs are very good substrates as are the small acyl-CoA metabolites
-
-
?
additional information
?
-
YciA is responsible for the efficient, indiscriminant CoA-regulated hydrolysis of cellular acyl-CoA thioesters in a wide range of bacteria and hypothesize that this activity may support membrane biogenesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the physiological role of thioesterase II in Escherichia coli is to prevent the abnormal accumulation of intracellular acyl-coenzyme A
-
-
?
additional information
?
-
the long, medium, and short chain fatty acyl-CoAs are very good substrates as are the small acyl-CoA metabolites
-
-
?
additional information
?
-
YciA is responsible for the efficient, indiscriminant CoA-regulated hydrolysis of cellular acyl-CoA thioesters in a wide range of bacteria and hypothesize that this activity may support membrane biogenesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PMSF
-
less effective than DFP, produces a 27% loss of activity under similar conditions
diisopropylfluorophosphate
-
1 mM DFP at 40 min at 25°C produces a 95% inhibition at palmityl thioesterase I
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
0.068
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
0.016
phenylacetyl-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
33
palmitoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
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
9.4
phenylacetyl-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
3.7
palmitoyl-CoA
pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay
additional information
additional information
inactive with substrates having acyl chains with fewer than 12 carbon atoms
-
additional information
additional information
-
inactive with substrates having acyl chains with fewer than 12 carbon atoms
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
also comparable activities observed with stearoyl-CoA and oleoyl-CoA
additional information
-
also comparable activities observed with stearoyl-CoA and oleoyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15160
His-tagged YciA protein, determined by electrospray ionization mass spectrometry
20000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
4 * 31842-32100, recombinant enzyme, electrospray ionization mass spectroscopy and SDS-PAGE
homohexamer
YciA determined by using equilibrium sedimentation techniques
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
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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.
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
the gene encoding YciA is amplified by PCR and expressed in Escherichia coli strain 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
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
Barnes jr., E.M.
Long-chain fatty acyl thioesterases I and II from Escherichia coli
Methods Enzymol.
35
102-109
1975
Escherichia coli
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, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus (Q9R0X4), Oryctolagus cuniculus, Rattus norvegicus
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)
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)
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
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)
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