| IED ID | IndEnz0010001024 |
| Enzyme Type ID | esterase001024 |
| Protein Name |
Cutinase est2 EC 3.1.1.74 Poly ethylene terephthalate hydrolase PET hydrolase PETase EC 3.1.1.101 TaCut2 |
| Gene Name | est2 est119 |
| Organism | Thermobifida alba (Thermomonospora alba) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida alba (Thermomonospora alba) |
| Enzyme Sequence | MSVTTPRRETSLLSRALRATAAAATAVVATVALAAPAQAANPYERGPNPTESMLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSAVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGAEYDTIASVTLHSKPFYNSIPSPTDKAYLELDGASHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVEEYRSTCPF |
| Enzyme Length | 300 |
| Uniprot Accession Number | F7IX06 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Nucleophile; /evidence=ECO:0000305|PubMed:30761732; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000305|PubMed:30761732; ACT_SITE 247; /note=Charge relay system; /evidence=ECO:0000305|PubMed:30761732 |
| Activity Regulation | ACTIVITY REGULATION: Activated by calcium ions (PubMed:22183084). Activated by magnesium ions (PubMed:22183084). Activated by manganese ions (PubMed:22183084). Inhibited by the serine hydrolase inhibitor phenylmethanesulfonyl fluoride (PMSF) (PubMed:22183084). Inhibited by the chelator ethylenediaminetetraacetic acid (EDTA) (PubMed:22183084). Inhibited by iron ions (PubMed:22183084). Inhibited by aluminum ions (PubMed:22183084). Inhibited by rubidium ions (PubMed:22183084). Inhibited by lithium ions (PubMed:22183084). {ECO:0000269|PubMed:22183084}. |
| Binding Site | BINDING 99; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 170; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 194; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000305|PubMed:20393707, ECO:0000305|PubMed:22183084};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000305|PubMed:20393707, ECO:0000305|PubMed:22183084}; 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:20393707, ECO:0000269|PubMed:22183084, ECO:0000269|PubMed:25910960, ECO:0000269|PubMed:33387709};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084, ECO:0000269|PubMed:25910960, ECO:0000269|PubMed:33387709}; CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:20393707, ECO:0000305|PubMed:22183084, ECO:0000305|PubMed:25910960, ECO:0000305|PubMed:33387709}; 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:20393707, ECO:0000269|PubMed:22183084};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47353; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; 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:20393707, ECO:0000269|PubMed:22183084};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47357; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; |
| DNA Binding | |
| EC Number | 3.1.1.74; 3.1.1.101 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (By similarity). Can also depolymerize the synthetic polyesters poly(epsilon-caprolactone) (PCL), poly(butylene succinate-co-adipate) (PBSA), poly(butylene succinate) (PBS), and poly(lactic acid) (PLA) (PubMed:20393707, PubMed:22183084). {ECO:0000250|UniProtKB:D4Q9N1, ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084, ECO:0000269|PubMed:25910960, ECO:0000269|PubMed:33387709}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:20393707}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:20393707}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (1); Disulfide bond (1); Metal binding (3); Mutagenesis (11); Signal peptide (1) |
| Keywords | 3D-structure;Calcium;Disulfide bond;Hydrolase;Metal-binding;Periplasm;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is not induced by the synthetic polyester poly(butylene succinate-co-adipate) (PBSA). {ECO:0000269|PubMed:25910960}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3VIS; 3WYN; 6AID; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,353 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.22 mM for pNP-acetate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=3.41 mM for pNP-butyrate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=2.37 mM for pNP-hexanoate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=1.87 mM for pNP-octanoate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; Note=kcat is 2.06 sec(-1) with pNP-acetate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 4.48 sec(-1) with pNP-butyrate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 3.28 sec(-1) with pNP-hexanoate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 2.45 sec(-1) with pNP-octanoate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). {ECO:0000269|PubMed:22183084}; |
| Metal Binding | METAL 213; /note="Calcium"; /evidence="ECO:0000269|PubMed:30761732, ECO:0007744|PDB:3WYN, ECO:0007744|PDB:6AID"; METAL 243; /note="Calcium"; /evidence="ECO:0000269|PubMed:30761732, ECO:0007744|PDB:3WYN, ECO:0007744|PDB:6AID"; METAL 292; /note="Calcium"; /evidence="ECO:0000269|PubMed:30761732, ECO:0007744|PDB:3WYN, ECO:0007744|PDB:6AID" |
| Rhea ID | RHEA:12957; RHEA:12958; RHEA:49528; RHEA:49529; RHEA:47348; RHEA:47349; RHEA:47352; RHEA:47353; RHEA:47356; RHEA:47357 |
| Cross Reference Brenda |