IED Industry Enzyme Database

Detail Information for IndEnz0005000744
IED ID IndEnz0005000744
Enzyme Type ID lipase000744
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;