| IED ID | IndEnz0010000492 |
| Enzyme Type ID | esterase000492 |
| Protein Name |
Cutinase EC 3.1.1.74 Poly ethylene terephthalate hydrolase PET hydrolase PETase EC 3.1.1.101 |
| Gene Name | TfH Tfu_0883 |
| Organism | Thermobifida fusca (strain YX) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida fusca (Thermomonospora fusca) Thermobifida fusca (strain YX) |
| Enzyme Sequence | MAVMTPRRERSSLLSRALQVTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF |
| Enzyme Length | 301 |
| Uniprot Accession Number | Q47RJ6 |
| Absorption | |
| Active Site | ACT_SITE 170; /note=Nucleophile; /evidence=ECO:0000305|PubMed:18658138; ACT_SITE 216; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 248; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7 |
| Activity Regulation | ACTIVITY REGULATION: Activated by magnesium ions (PubMed:25545638). Activated by calcium ions (PubMed:25545638). Inhibited by the serine hydrolase inhibitor phenylmethanesulfonyl fluoride (PMSF) (PubMed:18658138). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:25545638}. |
| Binding Site | BINDING 100; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 171; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 195; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7 |
| Calcium Binding | |
| catalytic Activity | 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:18658138, ECO:0000269|PubMed:20729325, ECO:0000269|PubMed:21594592, ECO:0000269|PubMed:21751386, ECO:0000269|PubMed:23603671, ECO:0000269|PubMed:25545638};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:20729325, ECO:0000269|PubMed:21751386, ECO:0000269|PubMed:25545638}; 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:0000269|PubMed:21751386, ECO:0000269|PubMed:25545638};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000269|PubMed:21751386, ECO:0000269|PubMed:25545638}; CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:20729325}; |
| 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:18658138, PubMed:20729325). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:18658138, PubMed:20729325, PubMed:21594592, PubMed:21751386, PubMed:23603671, PubMed:25545638). Also hydrolyzes the triglyceride triolein (PubMed:18658138, PubMed:20729325, PubMed:21751386) (Probable). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:21751386, PubMed:25545638). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:20729325, ECO:0000269|PubMed:21594592, ECO:0000269|PubMed:21751386, ECO:0000269|PubMed:23603671, ECO:0000269|PubMed:25545638, ECO:0000305|PubMed:23603671}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:20729325, ECO:0000269|PubMed:23603671}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:20729325, ECO:0000269|PubMed:23603671}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (1); Disulfide bond (1); Mutagenesis (4); Signal peptide (1) |
| Keywords | Disulfide bond;Hydrolase;Periplasm;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..40; /evidence=ECO:0000305|PubMed:18658138 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,218 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=640 uM for pNP-butanoate {ECO:0000269|PubMed:20729325}; KM=312 uM for pNP-butanoate (at 20 degrees Celsius and pH 8) {ECO:0000269|PubMed:23603671}; Note=kcat is 220 sec(-1) with pNP-butanoate as substrate (PubMed:20729325). kcat is 304 sec(-1) with pNP-butanoate as substrate (at 20 degrees Celsius and pH 8) (PubMed:23603671). {ECO:0000269|PubMed:20729325, ECO:0000269|PubMed:23603671}; |
| Metal Binding | |
| Rhea ID | RHEA:47348; RHEA:47349; RHEA:49528; RHEA:49529 |
| Cross Reference Brenda | 3.1.1.3;3.1.1.74; |