Reference on EC 3.1.2.2 - palmitoyl-CoA hydrolase and Organism(s) Escherichia coli and UniProt Accession P0A8Z0
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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), Mus musculus, 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), Escherichia coli
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
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
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)
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
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
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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