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Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)

 TESA_ECOLI              Reviewed;         208 AA.
P0ADA1; P29679; P37331; P77125; Q2MBT3;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
25-OCT-2017, entry version 98.
RecName: Full=Thioesterase 1/protease 1/lysophospholipase L1 {ECO:0000303|PubMed:15697222};
Short=TAP {ECO:0000303|PubMed:15697222};
AltName: Full=Acyl-CoA thioesterase 1 {ECO:0000303|PubMed:8098033};
Short=TESA {ECO:0000303|PubMed:8098033};
EC=3.1.2.2 {ECO:0000269|PubMed:4554913};
AltName: Full=Acyl-CoA thioesterase I {ECO:0000303|PubMed:8098033};
AltName: Full=Arylesterase {ECO:0000303|PubMed:9070299};
EC=3.1.1.2 {ECO:0000269|PubMed:9070299};
AltName: Full=Lysophospholipase L1 {ECO:0000303|PubMed:1864840};
EC=3.1.1.5 {ECO:0000305|PubMed:10423542, ECO:0000305|PubMed:1864840};
AltName: Full=Oleoyl-[acyl-carrier-protein] hydrolase {ECO:0000303|PubMed:4554913};
EC=3.1.2.14 {ECO:0000269|PubMed:4554913};
AltName: Full=Phospholipid degradation C {ECO:0000303|PubMed:1864840};
Short=Pldc {ECO:0000303|PubMed:1864840};
AltName: Full=Protease 1 {ECO:0000303|PubMed:4945109};
EC=3.4.21.- {ECO:0000305|PubMed:791643};
AltName: Full=Protease I {ECO:0000303|PubMed:4945109};
AltName: Full=Thioesterase I/protease I {ECO:0000303|PubMed:12846577};
Short=TEP-I {ECO:0000303|PubMed:12846577};
Flags: Precursor;
Name=tesA {ECO:0000303|PubMed:8098033};
Synonyms=apeA {ECO:0000303|PubMed:8432696},
pldC {ECO:0000303|PubMed:1864840}; OrderedLocusNames=b0494, JW0483;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
FUNCTION AS A THIOESTERASE, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, ACTIVE SITE, SUBUNIT, AND NOMENCLATURE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8098033;
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-38, FUNCTION
AS A PROTEASE, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBSTRATE
SPECIFICITY, AND NOMENCLATURE.
STRAIN=K12;
PubMed=8432696; DOI=10.1128/jb.175.4.1032-1037.1993;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
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:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 27-37, FUNCTION AS A LYSOPHOSPHOLIPASE, CATALYTIC
ACTIVITY, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT, AND
NOMENCLATURE.
STRAIN=K12;
PubMed=1864840;
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).
[7]
FUNCTION AS A PROTEASE, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
REGULATION.
PubMed=4945109;
Pacaud M., Uriel J.;
"Isolation and some propeties of a proteolytic enzyme from Escherichia
coli (protease I).";
Eur. J. Biochem. 23:435-442(1971).
[8]
FUNCTION AS A THIOESTERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=4554913;
Bonner W.M., Bloch K.;
"Purification and properties of fatty acyl thioesterase I from
Escherichia coli.";
J. Biol. Chem. 247:3123-3133(1972).
[9]
FUNCTION AS A LYSOPHOSPHOLIPASE, ENZYME REGULATION, AND SUBSTRATE
SPECIFICITY.
PubMed=238979;
Doi O., Nojima S.;
"Lysophospholipase of Escherichia coli.";
J. Biol. Chem. 250:5208-5214(1975).
[10]
FUNCTION AS A PROTEASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=791643;
Pacaud M., Sibilli S., Bras G.;
"Protease I from Escherichia coli. Some physicochemical properties and
substrate specificity.";
Eur. J. Biochem. 69:141-151(1976).
[11]
FUNCTION AS A THIOESTERASE, AND SUBSTRATE SPECIFICITY.
PubMed=8132479;
Cho H., Cronan J.E. Jr.;
"Protease I of Escherichia coli functions as a thioesterase in vivo.";
J. Bacteriol. 176:1793-1795(1994).
[12]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBSTRATE SPECIFICITY.
PubMed=9070299; DOI=10.1006/bbrc.1997.5797;
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).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=10423542;
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).
[14]
ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
REACTION MECHANISM.
PubMed=12846577; DOI=10.1021/bi027246w;
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).
[15]
MUTAGENESIS OF SER-36; GLY-70; ASN-99; ASP-180 AND HIS-183,
BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
PubMed=16515533; DOI=10.1042/BJ20051645;
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).
[16]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-208 OF WILD-TYPE AND
MUTANT PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE,
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
PubMed=12842470; DOI=10.1016/S0022-2836(03)00637-5;
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).
[17]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 27-208 OF WILD-TYPE AND
MUTANT PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF
LEU-135, AND ACTIVE SITE.
PubMed=15697222; DOI=10.1021/bi048109x;
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).
-!- FUNCTION: TesA is a multifunctional esterase that can act as a
thioesterase, lysophospholipase and protease (PubMed:8098033,
PubMed:8432696, PubMed:1864840, PubMed:4945109, PubMed:4554913,
PubMed:238979, PubMed:791643, PubMed:8132479, PubMed:9070299,
PubMed:10423542). TesA functions as a thioesterase specific for
fatty acyl thioesters of greater than ten carbons, with highest
activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA
(PubMed:8098033, PubMed:4554913, PubMed:8132479, PubMed:9070299,
PubMed:10423542). TesA also possesses an arylesterase activity
towards short acyl-chain aromatic esters such as alpha-naphthyl
acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl
acetate (PubMed:9070299). Also able to hydrolyze short acyl-chain
triacylglycerols such as triacetin and tributyrin, and p-
nitrophenyl esters such as p-nitrophenyl hexanoate and p-
nitrophenyl butyrate (PubMed:9070299). The protease activity is
mainly active on small peptides (PubMed:8432696, PubMed:9070299).
TesA is also able to hydrolyze p-nitrophenyl esters of N-
substituted amino acids such as N-benzyloxycarbonyl-L-Phe-p-
nitrophenyl ester (Z-L-Phe-ONp) and N-benzyloxycarbonyl-L-Tyr-p-
nitrophenyl ester (Z-L-Tyr-ONp), however it is unable to hydrolyze
N-acetyl-L-Phe ethyl ester and its Tyr analog (PubMed:8432696,
PubMed:791643, PubMed:10423542). TesA also hydrolyzes N-
benzyloxycarbonyl-L-Phe beta-nitrophenyl ester (Cbz-Phe-ONap) and
N-acetyl-DL-Phe-2-naphthyl ester (chymotrypsin-like specificity)
(PubMed:8432696, PubMed:4945109). Shows a slow proteolytic
activity against denatured casein (PubMed:4945109). The
lysophospholipase activity of TesA is able to hydrolyze 1-
palmitoyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-
phosphoglycerol, 1- and 2-acyl-sn-glycero-3-phosphoethanolamine
(PubMed:1864840, PubMed:238979, PubMed:10423542).
{ECO:0000269|PubMed:10423542, ECO:0000269|PubMed:1864840,
ECO:0000269|PubMed:238979, ECO:0000269|PubMed:4554913,
ECO:0000269|PubMed:4945109, ECO:0000269|PubMed:791643,
ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8132479,
ECO:0000269|PubMed:8432696, ECO:0000269|PubMed:9070299}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
{ECO:0000269|PubMed:4554913}.
-!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
glycerophosphocholine + a carboxylate.
{ECO:0000305|PubMed:10423542, ECO:0000305|PubMed:1864840}.
-!- CATALYTIC ACTIVITY: A phenyl acetate + H(2)O = a phenol + acetate.
{ECO:0000269|PubMed:9070299}.
-!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-
carrier-protein] + oleate. {ECO:0000269|PubMed:4554913}.
-!- ENZYME REGULATION: Thioesterase activity is inhibited by
iodoacetamide and photoactivated methylene blue, and slowly
inhibited by 2,4-dinitrofluorobenzene (PubMed:4554913). Protease
and lysophospholipase activities are inhibited by
diisopropylfluorophosphate (DFP) (PubMed:1864840, PubMed:4945109,
PubMed:238979). Lysophospholipase activity is inhibited by Fe(2+),
Fe(3+) and Al(3+) ions (PubMed:238979). Diethyl p-nitrophenyl
phosphate (DENP) irreversibly inhibits both the protease and
thioesterase activities (PubMed:12846577).
{ECO:0000269|PubMed:12846577, ECO:0000269|PubMed:1864840,
ECO:0000269|PubMed:238979, ECO:0000269|PubMed:4554913,
ECO:0000269|PubMed:4945109}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.5 uM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester
{ECO:0000269|PubMed:9070299};
KM=3.8 uM for oleyl-ACP {ECO:0000269|PubMed:4554913};
KM=4 uM for oleyl-CoA {ECO:0000269|PubMed:4554913};
KM=4 uM for palmitoleoyl-CoA {ECO:0000269|PubMed:4554913};
KM=4.6 uM for cis-vaccenoyl-CoA {ECO:0000269|PubMed:4554913};
KM=6.2 uM for palmitoyl-CoA {ECO:0000269|PubMed:4554913};
KM=6.4 uM for myristoyl-CoA {ECO:0000269|PubMed:4554913};
KM=7.2 uM for palmitoyl-CoA {ECO:0000269|PubMed:9070299};
KM=7.7 uM for stearoyl-CoA {ECO:0000269|PubMed:4554913};
KM=9.9 uM for arachidoyl-CoA {ECO:0000269|PubMed:4554913};
KM=11.5 uM for decanoyl-CoA {ECO:0000269|PubMed:4554913};
KM=13.2 uM for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl
ester {ECO:0000269|PubMed:9070299};
KM=27.3 uM for hexanoyl-CoA {ECO:0000269|PubMed:4554913};
KM=110 uM for oleyl pantetheine {ECO:0000269|PubMed:4554913};
KM=146 uM for lauroyl-CoA (at pH 7 and 37 degrees Celsius)
{ECO:0000269|PubMed:16515533};
KM=174 uM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester (at
pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:16515533};
KM=200 uM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester
{ECO:0000269|PubMed:791643};
KM=730 uM for diethyl p-nitrophenyl phosphate
{ECO:0000269|PubMed:12846577};
KM=617.8 uM for p-nitrophenyl decaonate
{ECO:0000269|PubMed:9070299};
KM=870 uM for p-nitrophenyl butyrate (at pH 7 and 37 degrees
Celsius) {ECO:0000269|PubMed:16515533};
KM=1.46 mM for p-nitrophenyl butyrate
{ECO:0000269|PubMed:9070299};
Vmax=25 umol/min/mg enzyme with N-benzyloxycarbonyl-L-tyrosine-
p-nitrophenyl ester as substrate {ECO:0000269|PubMed:791643};
Vmax=0.33 umol/min/mg enzyme with diethyl p-nitrophenyl
phosphate as substrate {ECO:0000269|PubMed:12846577};
Vmax=30.1 pmol/min/mg enzyme with palmitoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=20.9 pmol/min/mg enzyme with myristoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=19.7 pmol/min/mg enzyme with stearoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=19.3 pmol/min/mg enzyme with cis-vaccenoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=17 pmol/min/mg enzyme with arachidoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=15.7 pmol/min/mg enzyme with palmitoleoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=14 pmol/min/mg enzyme with oleyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=9.6 pmol/min/mg enzyme with decanoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=7.7 pmol/min/mg enzyme with hexanoyl-CoA as substrate
{ECO:0000269|PubMed:4554913};
Vmax=7.6 pmol/min/mg enzyme with oleyl pantetheine as substrate
{ECO:0000269|PubMed:4554913};
Vmax=0.4 pmol/min/mg enzyme with oleyl-ACP as substrate
{ECO:0000269|PubMed:4554913};
Note=Kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-
nitrophenyl ester as substrate (PubMed:16515533). Kcat is 62.4
sec(-1) for p-nitrophenyl butyrate as substrate
(PubMed:9070299). Kcat is 15.29 sec(-1) for p-nitrophenyl
butyrate as substrate (PubMed:16515533). Kcat is 14.1 sec(-1)
for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as
substrate (PubMed:9070299). Kcat is 10.13 sec(-1) for lauroyl-
CoA as substrate (PubMed:16515533). Kcat is 5.1 sec(-1) for p-
nitrophenyl decaonate as substrate (PubMed:9070299). Kcat is 2.6
sec(-1) for palmitoyl-CoA as substrate (PubMed:9070299). Kcat is
2.3 sec(-1) for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl
ester as substrate (PubMed:9070299).
{ECO:0000269|PubMed:16515533, ECO:0000269|PubMed:9070299};
pH dependence:
Optimum pH is 7.5-8.4 (PubMed:4945109, PubMed:4554913,
PubMed:12846577). Stable between pH 6.1 and 12, however, below
pH 6.0, thioesterase rapidly loses activity (PubMed:4554913).
{ECO:0000269|PubMed:12846577, ECO:0000269|PubMed:4554913,
ECO:0000269|PubMed:4945109};
Temperature dependence:
Protease is stable up to 50 degrees Celsius.
{ECO:0000269|PubMed:4945109};
-!- SUBUNIT: Monomer or homotetramer. {ECO:0000269|PubMed:12842470,
ECO:0000269|PubMed:1864840, ECO:0000269|PubMed:4554913,
ECO:0000269|PubMed:791643, ECO:0000269|PubMed:8098033}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8098033,
ECO:0000269|PubMed:8432696}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show
thioesterase activity and have a little protease activity against
Cbz-Phe-ONap. No effect on the cell growth and fatty acid
composition. {ECO:0000269|PubMed:8098033,
ECO:0000269|PubMed:8432696}.
-!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB40248.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L06182; AAA24664.1; -; Genomic_DNA.
EMBL; D13180; BAA02475.1; -; Genomic_DNA.
EMBL; U82664; AAB40248.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73596.1; -; Genomic_DNA.
EMBL; AP009048; BAE76273.1; -; Genomic_DNA.
PIR; A49699; A49699.
PIR; PX0045; PX0045.
RefSeq; NP_415027.1; NC_000913.3.
RefSeq; WP_001297298.1; NZ_LN832404.1.
PDB; 1IVN; X-ray; 1.90 A; A=27-208.
PDB; 1J00; X-ray; 2.00 A; A=27-208.
PDB; 1JRL; X-ray; 1.95 A; A=27-208.
PDB; 1U8U; X-ray; 2.08 A; A=27-208.
PDB; 1V2G; X-ray; 2.00 A; A=27-208.
PDB; 5TIC; X-ray; 1.65 A; A/B=28-208.
PDB; 5TID; X-ray; 1.20 A; A=28-208.
PDB; 5TIE; X-ray; 1.15 A; A=28-208.
PDB; 5TIF; X-ray; 0.97 A; A=28-208.
PDBsum; 1IVN; -.
PDBsum; 1J00; -.
PDBsum; 1JRL; -.
PDBsum; 1U8U; -.
PDBsum; 1V2G; -.
PDBsum; 5TIC; -.
PDBsum; 5TID; -.
PDBsum; 5TIE; -.
PDBsum; 5TIF; -.
ProteinModelPortal; P0ADA1; -.
SMR; P0ADA1; -.
BioGrid; 4259854; 5.
STRING; 316385.ECDH10B_0451; -.
DrugBank; DB02364; 2-Amino-3-(Diethoxy-Phosphoryloxy)-Propionic Acid.
DrugBank; DB04519; Caprylic acid.
SWISS-2DPAGE; P0ADA1; -.
PaxDb; P0ADA1; -.
PRIDE; P0ADA1; -.
EnsemblBacteria; AAC73596; AAC73596; b0494.
EnsemblBacteria; BAE76273; BAE76273; BAE76273.
GeneID; 945127; -.
KEGG; ecj:JW0483; -.
KEGG; eco:b0494; -.
PATRIC; fig|511145.12.peg.515; -.
EchoBASE; EB1504; -.
EcoGene; EG11542; tesA.
eggNOG; ENOG4108UJV; Bacteria.
eggNOG; COG2755; LUCA.
HOGENOM; HOG000261382; -.
InParanoid; P0ADA1; -.
KO; K10804; -.
PhylomeDB; P0ADA1; -.
BioCyc; EcoCyc:THIOESTERI-MONOMER; -.
BioCyc; MetaCyc:THIOESTERI-MONOMER; -.
BRENDA; 3.1.1.5; 2026.
BRENDA; 3.1.2.2; 2026.
SABIO-RK; P0ADA1; -.
EvolutionaryTrace; P0ADA1; -.
PRO; PR:P0ADA1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:EcoCyc.
GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0004622; F:lysophospholipase activity; IDA:EcoCyc.
GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:EcoCyc.
GO; GO:0008233; F:peptidase activity; IDA:EcoCyc.
GO; GO:0004620; F:phospholipase activity; IDA:EcoCyc.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
Gene3D; 3.40.50.1110; -; 1.
InterPro; IPR008265; Lipase_GDSL_AS.
InterPro; IPR013830; SGNH_hydro.
InterPro; IPR036514; SGNH_hydro_sf.
Pfam; PF13472; Lipase_GDSL_2; 1.
SUPFAM; SSF52266; SSF52266; 1.
PROSITE; PS01098; LIPASE_GDSL_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Hydrolase;
Periplasm; Protease; Reference proteome; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:1864840,
ECO:0000269|PubMed:8098033,
ECO:0000269|PubMed:8432696}.
CHAIN 27 208 Thioesterase 1/protease
1/lysophospholipase L1.
/FTId=PRO_0000017848.
ACT_SITE 36 36 Nucleophile.
{ECO:0000269|PubMed:15697222,
ECO:0000269|PubMed:16515533,
ECO:0000305|PubMed:12842470,
ECO:0000305|PubMed:12846577,
ECO:0000305|PubMed:8098033}.
ACT_SITE 180 180 {ECO:0000269|PubMed:15697222,
ECO:0000269|PubMed:16515533,
ECO:0000305|PubMed:12842470,
ECO:0000305|PubMed:12846577}.
ACT_SITE 183 183 {ECO:0000269|PubMed:15697222,
ECO:0000269|PubMed:16515533,
ECO:0000305|PubMed:12842470,
ECO:0000305|PubMed:12846577}.
BINDING 70 70 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:15697222}.
BINDING 99 99 Substrate. {ECO:0000269|PubMed:15697222}.
MUTAGEN 36 36 S->A: Loss of hydrolysis activity.
{ECO:0000269|PubMed:16515533}.
MUTAGEN 70 70 G->A: Retains weak hydrolysis activity.
{ECO:0000269|PubMed:16515533}.
MUTAGEN 99 99 N->A: Retains weak hydrolysis activity.
{ECO:0000269|PubMed:16515533}.
MUTAGEN 135 135 L->P: Abolishes switch loop movement.
Lowers activity towards substrates with
long acyl chains.
{ECO:0000269|PubMed:15697222}.
MUTAGEN 180 180 D->A: Retains weak hydrolysis activity.
{ECO:0000269|PubMed:16515533}.
MUTAGEN 183 183 H->A: Loss of hydrolysis activity.
{ECO:0000269|PubMed:16515533}.
STRAND 28 34 {ECO:0000244|PDB:1IVN}.
HELIX 36 39 {ECO:0000244|PDB:1IVN}.
STRAND 41 43 {ECO:0000244|PDB:1IVN}.
HELIX 45 47 {ECO:0000244|PDB:1IVN}.
HELIX 49 56 {ECO:0000244|PDB:1IVN}.
TURN 57 60 {ECO:0000244|PDB:1U8U}.
STRAND 61 65 {ECO:0000244|PDB:1IVN}.
HELIX 73 87 {ECO:0000244|PDB:1IVN}.
STRAND 90 95 {ECO:0000244|PDB:1IVN}.
TURN 98 101 {ECO:0000244|PDB:1IVN}.
STRAND 102 104 {ECO:0000244|PDB:1IVN}.
HELIX 107 123 {ECO:0000244|PDB:1IVN}.
STRAND 127 131 {ECO:0000244|PDB:1IVN}.
HELIX 137 139 {ECO:0000244|PDB:1IVN}.
HELIX 141 157 {ECO:0000244|PDB:1IVN}.
HELIX 167 171 {ECO:0000244|PDB:1IVN}.
HELIX 174 176 {ECO:0000244|PDB:1IVN}.
STRAND 181 184 {ECO:0000244|PDB:1IVN}.
HELIX 186 188 {ECO:0000244|PDB:1IVN}.
HELIX 189 200 {ECO:0000244|PDB:1IVN}.
TURN 201 204 {ECO:0000244|PDB:1IVN}.
SEQUENCE 208 AA; 23622 MW; CD03F23EA39541F1 CRC64;
MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP ALLNDKWQSK
TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND GLRGFQPQQT EQTLRQILQD
VKAANAEPLL MQIRLPANYG RRYNEAFSAI YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD
GIHPNRDAQP FIADWMAKQL QPLVNHDS


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