Sequence of TESA_ECOLI
EC Number:3.1.2.14
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate
Other sequences found for EC No. 3.1.2.14
General information:
Sequence
0 MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP ALLNDKWQSK
60 TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND GLRGFQPQQT EQTLRQILQD
120 VKAANAEPLL MQIRLPANYG RRYNEAFSAI YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD
180 GIHPNRDAQP FIADWMAKQL QPLVNHDS
Download this sequence
in fasta formatDownload all sequences for 3.1.2.14
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
745122
Cho H.,Cronan J.E. Jr.
Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme.
J. Biol. Chem.
268
9238-9245
1993
745123
Ichihara S.,Matsubara Y.,Kato C.,Akasaka K.,Mizushima S.
Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants.
J. Bacteriol.
175
1032-1037
1993
745125
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
745126
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
745127
Karasawa K.,Kudo I.,Kobayashi T.,Homma H.,Chiba N.,Mizushima H.,Inoue K.,Nojima S.
Lysophospholipase L1 from Escherichia coli K-12 overproducer.
J. Biochem.
109
288-293
1991
745128
Pacaud M.,Uriel J.
Isolation and some propeties of a proteolytic enzyme from Escherichia coli (protease I).
Eur. J. Biochem.
23
435-442
1971
745129
Bonner W.M.,Bloch K.
Purification and properties of fatty acyl thioesterase I from Escherichia coli.
J. Biol. Chem.
247
3123-3133
1972
745131
Pacaud M.,Sibilli S.,Bras G.
Protease I from Escherichia coli. Some physicochemical properties and substrate specificity.
Eur. J. Biochem.
69
141-151
1976
745132
Cho H.,Cronan J.E. Jr.
Protease I of Escherichia coli functions as a thioesterase in vivo.
J. Bacteriol.
176
1793-1795
1994
745133
Lee Y.L.,Chen J.C.,Shaw J.F.
The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates.
Biochem. Biophys. Res. Commun.
231
452-456
1997
745134
Karasawa K.,Yokoyama K.,Setaka M.,Nojima S.
The Escherichia coli pldC gene encoding lysophospholipase L(1) is identical to the apeA and tesA genes encoding protease I and thioesterase I, respectively.
J. Biochem.
126
445-448
1999
745135
Tyukhtenko S.I.,Litvinchuk A.V.,Chang C.F.,Lo Y.C.,Lee S.J.,Shaw J.F.,Liaw Y.C.,Huang T.H.
Sequential structural changes of Escherichia coli thioesterase/protease I in the serial formation of Michaelis and tetrahedral complexes with diethyl p-nitrophenyl phosphate.
Biochemistry
42
8289-8297
2003
745136
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
745137
Lo Y.-C.,Lin S.-C.,Shaw J.-F.,Liaw Y.-C.
Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network.
J. Mol. Biol.
330
539-551
2003
745138
Lo Y.-C.,Lin S.-C.,Shaw J.-F.,Liaw Y.-C.
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement.
Biochemistry
44
1971-1979
2005
