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Synonyms
thioesterase, palmitoyl-coa hydrolase, acot7, thioesterase ii, acot1, type ii fas, acot2, thioesterase i, mte-i, cte-i,
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acyl CoA hydrolase
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acyl coenzyme A hydrolase
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acyl coenzyme A thioesterase
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acyl-CoA thioesterase
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brain acyl-CoA hydrolase
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fatty acyl thioesterase I
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HIV-Nef associated acyl coA thioesterase
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hydrolase, acyl coenzyme A
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hydrolase, palmitoyl coenzyme A
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long chain acyl-CoA hydrolase
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long chain acyl-CoA thioesterase
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long chain fatty-acyl-CoA hydrolase
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long chain fatty-acyl-CoA thioesterase
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mitochondrial acyl-CoA thioesterase
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palmitoyl coenzyme A hydrolase
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palmitoyl thioesterase
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palmitoyl-CoA deacylase
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palmitoyl-CoA hydrolase
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palmityl coenzyme A deacylase
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palmityl thioesterase
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palmityl thioesterase I
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palmityl thioesterase II
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thioesterase I/protease I/lysophospholipase L1
multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophospholipase activities
type II fatty acid synthase
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very long chain acyl-CoA thioesterase
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thioesterase I
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thioesterase I
multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophospholipase activities
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0.00013 - 0.006
fatty-acyl-CoA thioester
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0.059 - 0.185
lauroyl-CoA
0.043 - 0.174
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
0.61 - 1.88
p-nitrophenyl butyrate
0.059
lauroyl-CoA
37°C, pH 7, mutant enzyme D154A
0.073
lauroyl-CoA
mutant enzyme P110A/L109P
0.075
lauroyl-CoA
37°C, pH 7, mutant enzyme G44A
0.085
lauroyl-CoA
37°C, pH 7, mutant enzyme N73A
0.113
lauroyl-CoA
mutant enzyme P110A
0.127
lauroyl-CoA
37°C, pH 7, mutant enzyme, S10A
0.146
lauroyl-CoA
native enzyme
0.146
lauroyl-CoA
37°C, pH 7, wild-type enzyme
0.185
lauroyl-CoA
mutant enzyme L109P
0.043
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme D154A
0.044
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme N73A
0.06
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme G44A
0.061
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme, S10A
0.174
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, wild-type enzyme
0.61
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme H157A
0.87
p-nitrophenyl butyrate
37°C, pH 7, wild-type enzyme
1.1
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme G44A
1.55
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme S10A
1.66
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme N73A
1.88
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme D154A
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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
0.052 - 2.1
lauroyl-CoA
native enzyme
0.052 - 2.1
lauroyl-CoA
37°C, pH 7, wild-type enzyme
0.057
lauroyl-CoA
37°C, pH 7, mutant enzyme, S10A
0.45
lauroyl-CoA
37°C, pH 7, mutant enzyme D154A
0.57
lauroyl-CoA
mutant enzyme L109P
0.77
lauroyl-CoA
37°C, pH 7, mutant enzyme G44A
0.84
lauroyl-CoA
mutant enzyme P110A/L109P
1.14
lauroyl-CoA
37°C, pH 7, mutant enzyme N73A
3.8
lauroyl-CoA
mutant enzyme P110A
10.13
lauroyl-CoA
native enzyme
10.13
lauroyl-CoA
37°C, pH 7, wild-type enzyme
0.02
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme, S10A
0.031 - 0.51
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme G44A
6.44
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme D154A
7.71
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme G44A
7.81
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme N73A
23.8
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, wild-type enzyme
88.99
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, wild-type enzyme
0.0093
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme H157A
0.16
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme S10A
0.41
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme N73A
0.55
p-nitrophenyl butyrate
37°C, pH 7, wild-type enzyme
3.16
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme G44A
5.98
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme D154A
11.99
p-nitrophenyl butyrate
37°C, pH 7, mutant enzyme N73A
15.29
p-nitrophenyl butyrate
37°C, pH 7, wild-type enzyme
additional information
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
37°C, pH 7, mutant enzyme D154A
additional information
N-carbobenzoxy-L-tyrosine p-nitrophenyl ester
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37°C, pH 7, mutant enzyme D154A
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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
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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
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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
brenda
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
brenda
Barnes jr., E.M.
Long-chain fatty acyl thioesterases I and II from Escherichia coli
Methods Enzymol.
35
102-109
1975
Escherichia coli
brenda
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), Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
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brenda