| IED ID | IndEnz0010001025 |
| Enzyme Type ID | esterase001025 |
| Protein Name |
Cutinase 1 EC 3.1.1.74 Poly ethylene terephthalate hydrolase PET hydrolase PETase EC 3.1.1.101 Fragment |
| Gene Name | cut1 |
| Organism | Thermobifida cellulosilytica |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida cellulosilytica |
| Enzyme Sequence | MANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF |
| Enzyme Length | 262 |
| Uniprot Accession Number | E9LVH8 |
| Absorption | |
| Active Site | ACT_SITE 131; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 177; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 209; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7 |
| Activity Regulation | |
| Binding Site | BINDING 61; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 132; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 156; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7 |
| Calcium Binding | |
| catalytic Activity | 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:23592055, ECO:0000269|Ref.1, ECO:0000305|PubMed:28671263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; 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:23592055, ECO:0000269|PubMed:23718548, ECO:0000269|Ref.1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|PubMed:23718548, ECO:0000269|Ref.1}; 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:23592055, ECO:0000269|Ref.1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000269|PubMed:23592055, ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:23592055, ECO:0000305|PubMed:28671263, ECO:0000305|Ref.1}; |
| 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 (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23718548, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23718548, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263). {ECO:0000269|PubMed:23592055, ECO:0000269|PubMed:23718548, ECO:0000269|PubMed:28671263, ECO:0000269|Ref.1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (1); Disulfide bond (1); Non-terminal residue (1) |
| Keywords | 3D-structure;Disulfide bond;Hydrolase;Periplasm;Secreted;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5LUI; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,306 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=127 uM for pNP-acetate (at 25 degrees Celsius and pH 7) {ECO:0000269|Ref.1}; KM=1.5 mM for pNP-acetate (at 25 degrees Celsius and pH 7) {ECO:0000269|PubMed:23592055}; KM=1483 uM for pNP-butanoate (at 25 degrees Celsius and pH 7) {ECO:0000269|Ref.1}; KM=800 uM for pNP-butanoate {ECO:0000269|PubMed:23718548}; KM=800 uM for pNP-butanoate (at 25 degrees Celsius and pH 7) {ECO:0000269|PubMed:23592055}; Note=kcat is 211.9 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 436 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 195.1 sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 325 sec(-1) with pNP-butanoate as substrate (PubMed:23718548). kcat is 327 sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). {ECO:0000269|PubMed:23592055, ECO:0000269|PubMed:23718548, ECO:0000269|Ref.1}; |
| Metal Binding | |
| Rhea ID | RHEA:49528; RHEA:49529; RHEA:47348; RHEA:47349; RHEA:12957; RHEA:12958 |
| Cross Reference Brenda | 3.1.1.101;3.1.1.74; |