IED ID | IndEnz0010001644 |
Enzyme Type ID | esterase001644 |
Protein Name |
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 |
Gene Name | tesA apeA pldC b0494 JW0483 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MMNFNNVFRWHLPFLFLVLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQWMQDDGIHPNRDAQPFIADWMAKQLQPLVNHDS |
Enzyme Length | 208 |
Uniprot Accession Number | P0ADA1 |
Absorption | |
Active Site | ACT_SITE 36; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577, ECO:0000305|PubMed:8098033"; ACT_SITE 180; /evidence="ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577"; ACT_SITE 183; /evidence="ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577" |
Activity Regulation | ACTIVITY 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}. |
Binding Site | BINDING 70; /note=Substrate; via amide nitrogen; /evidence=ECO:0000269|PubMed:15697222; BINDING 99; /note=Substrate; /evidence=ECO:0000269|PubMed:15697222 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; Evidence={ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:9070299};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:9070299};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15058; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H2O = (11Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:65240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30827, ChEBI:CHEBI:57287, ChEBI:CHEBI:75121; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65241; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:16515533};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence={ECO:0000269|PubMed:4554913};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000305|PubMed:10423542, ECO:0000305|PubMed:1864840}; CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:9070299}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:16515533, ECO:0000269|PubMed:9070299}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:9070299}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:9070299}; |
DNA Binding | |
EC Number | 3.1.2.2; 3.1.1.2; 3.1.1.5; 3.1.2.14; 3.4.21.- |
Enzyme Function | 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-vaccenoyl-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}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Protease is stable up to 50 degrees Celsius. {ECO:0000269|PubMed:4945109}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: 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}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (6); Binding site (2); Chain (1); Erroneous initiation (1); Helix (11); Mutagenesis (6); Signal peptide (1) |
Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Lipid metabolism;Periplasm;Protease;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8432696}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..26; /evidence="ECO:0000269|PubMed:1864840, ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8432696" |
Structure 3D | X-ray crystallography (11) |
Cross Reference PDB | 1IVN; 1J00; 1JRL; 1U8U; 1V2G; 5TIC; 5TID; 5TIE; 5TIF; 6LFB; 6LFC; |
Mapped Pubmed ID | 29375928; 32339761; |
Motif | |
Gene Encoded By | |
Mass | 23,622 |
Kinetics | 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 oleoyl-ACP {ECO:0000269|PubMed:4554913}; KM=4 uM for oleoyl-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 arachidonoyl-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 oleoyl 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 decanoate {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 arachidonoyl-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 oleoyl-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 oleoyl pantetheine as substrate {ECO:0000269|PubMed:4554913}; Vmax=0.4 pmol/min/mg enzyme with oleoyl-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 decanoate 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}; |
Metal Binding | |
Rhea ID | RHEA:16781; RHEA:16782; RHEA:16645; RHEA:16646; RHEA:40131; RHEA:40132; RHEA:30139; RHEA:30140; RHEA:40139; RHEA:40140; RHEA:15057; RHEA:15058; RHEA:65240; RHEA:65241; RHEA:40119; RHEA:40120; RHEA:40151; RHEA:40152; RHEA:30135; RHEA:30136; RHEA:40059; RHEA:40060; RHEA:40115; RHEA:40116; RHEA:15177; RHEA:17309; RHEA:47348; RHEA:47352; RHEA:47356 |
Cross Reference Brenda | 3.1.1.5;3.1.2.2; |