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Information on EC 3.1.2.2 - palmitoyl-CoA hydrolase and Organism(s) Escherichia coli and UniProt Accession P0A8Z0

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.2 palmitoyl-CoA hydrolase
IUBMB Comments
Also hydrolyses CoA thioesters of other long-chain fatty acids.
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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
thioesterase, palmitoyl-coa hydrolase, acot7, thioesterase ii, acot1, type ii fas, acot2, thioesterase i, mte-i, cte-i, 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 thioesterase
-
-
-
0
brain acyl-CoA hydrolase
-
-
-
0
esterase
276379
-
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
TAP
282014
-
TE
-
-
-
0
TE-II
-
-
-
0
thioesterase
276383
-
thioesterase B
-
-
-
0
thioesterase I
thioesterase I/protease I/lysophospholipase L1
282014
multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophospholipase activities
thioesterase II
-
-
-
0
type II FAS
246
-
type II fatty acid synthase
246
-
very long chain acyl-CoA thioesterase
-
-
-
0
ZAP128
-
-
-
0
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + H2O = CoA + palmitate
show the reaction diagram
specific catalyzation of the deacylation of long-chain fatty acyl-CoA thioesters, enzyme possesses a Ser-His-Asp catalytic triad
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA hydrolase
Also hydrolyses CoA thioesters of other long-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
37270-64-7
EC 3.1.2.2
9025-87-0
-
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
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
malonyl-CoA + H2O
malonate + CoA
show the reaction diagram
-
-
-
?
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester + H2O
N-carbobenzoxy-L-tyrosine + p-nitrophenol
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
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
palmitoleoyl-CoA + H2O
CoA + palmitoleoate
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
palmitoyl-CoA + H2O
palmitate + CoA
show the reaction diagram
-
-
-
?
stearoyl-CoA + H2O
CoA + stearate
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
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + H2O
CoA + stearate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013 - 0.006
fatty-acyl-CoA thioester
-
-
0.059 - 0.185
lauroyl-CoA
0.043 - 0.174
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
0.61 - 1.88
p-nitrophenyl butyrate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052 - 10.13
lauroyl-CoA
0.02 - 88.99
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
0.0093 - 15.29
p-nitrophenyl butyrate
additional information
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
93.8
purified recombinant enzyme
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
122000
-
gel filtration, thioesterase I
123000
recombinant enzyme, native PAGE
20000
20000 - 23000
-
gel filtration
30000
-
4 * 30000, SDS-PAGE
90000
-
gel filtration, palmityl thioesterase II
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
purified recombinant His-tagged enzyme, 76.8 mg/ml, hanging-drop vapour-diffusion method, protein solution: 10 mM sodium phosphate, pH 7.0, plus equal volme of reservoir solution: 0.2 M ammonium sulfate, 27% w/w PEG-MME 5K, 0.1 M 2-[N-morpholino]ethanesulfonic acid, pH 6.5, room temperature, crystals appeared after 7-21 d, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D154A
kcat/KM for p-nitrophenyl butyrate is 18% of wild-type value. kcat/KM for lauroyl-CoA is 11% of wild-type value. kcat/KM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester is 29% of wild-type value
G44A
kcat/KM for p-nitrophenyl butyrate is 16% of wild-type value. kcat/KM for lauroyl-CoA is 15% of wild-type value. kcat/KM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester is 25% of wild-type value
H157A
kcat/KM for p-nitrophenyl butyrate is 0.09% of wild-type value
L109P
mutation shifts the substrate-preference from medium-to-long acyl chains to shorter acyl-chains of triglyceride and p-nitrophenyl ester, and increases the preference for aromatic-amino acid-derived esters. kcat for lauroyl-CoA is 17.8fold lower than wild-type value, Km-value for lauroyl-CoA is 1.3fold higher than wild-type value
N73A
kcat/KM for p-nitrophenyl butyrate is 41% of wild-type value. kcat/KM for lauroyl-CoA is 19% of wild-type value. kcat/KM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester is 35% of wild-type value
P110A
kcat for lauroyl-CoA is 2.7fold lower than wild-type value, Km-value for lauroyl-CoA is 1.3fold lower than wild-type value
P110A/L109P
kcat for lauroyl-CoA is 12fold lower than wild-type value, Km-value for lauroyl-CoA is 2fold lower than wild-type value
S10A
kcat/KM for p-nitrophenyl butyrate is 0.57% of wild-type value. kcat/KM for lauroyl-CoA is 0.6% of wild-type value. kcat/KM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester is 0.06% of wild-type value
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
646120
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C over 1 month
-
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
20fold, palmityl thioesterase II, palmityl thioesterase I
-
native wild-type: 8000fold to homogeneity
recombinant wild-type: 4fold to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain BY4741
-
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
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), Mus musculus
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), Escherichia coli
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), Escherichia coli
Manually annotated by BRENDA team
Lo, Y.C.; Lee, Y.L.; Shaw, J.F.; Liaw, Y.C.
Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli
Acta Crystallogr. Sect. D
56
756-757
2000
Escherichia coli
Manually annotated by BRENDA team
Kuznetsova, E.; Proudfoot, M.; Sanders, S.A.; Reinking, J.; Savchenko, A.; Arrowsmith, C.H.; Edwards, A.M.; Yakunin, A.F.
Enzyme genomics: Application of general enzymatic screens to discover new enzymes
FEMS Microbiol. Rev.
29
263-279
2005
Escherichia coli, Escherichia coli (P0A8Y8), Escherichia coli (P0A8Z0), Escherichia coli (P0A8Z3), Escherichia coli (P33018), Escherichia coli (P37355), Escherichia coli (P39298), Escherichia coli (P46130), Escherichia coli (P75736), Escherichia coli (P76561), Escherichia coli (P77781)
Manually annotated by BRENDA team
Lee, L.C.; Lee, Y.L.; Leu, R.J.; Shaw, J.F.
Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1
Biochem. J.
397
69-76
2006
Escherichia coli (P0ADA1), Escherichia coli
Manually annotated by BRENDA team
Lee, L.; Liaw, Y.; Lee, Y.; Shaw, J.
Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1
Biochim. Biophys. Acta
1774
959-967
2007
Escherichia coli (P0ADA1), Escherichia coli
Manually annotated by BRENDA team
Fernandez-Moya, R.; Leber, C.; Cardenas, J.; Da Silva, N.
Functional replacement of the Saccharomyces cerevisiae fatty acid synthase with a bacterial type II system allows flexible product profiles
Biotechnol. Bioeng.
112
2618-2623
2015
Escherichia coli, Escherichia coli XL1-Blue
-
Manually annotated by BRENDA team
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