Detail Information for IndEnz0010001047
IED ID IndEnz0010001047
Enzyme Type ID esterase001047
Protein Name Cutinase est1
EC 3.1.1.74
Poly
ethylene terephthalate
hydrolase
PET hydrolase
PETase
EC 3.1.1.101
Gene Name est1
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 MSVTTPRREASLLSRAVAVAAAAAATVALAAPAQAANPYERGPNPTESMLEARSGPFSVSEERASRLGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSSVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGADLDTIAPVSSHSEPFYNSIPSSTDKAYLELNNATHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVDEYRSTCPF
Enzyme Length 296
Uniprot Accession Number D4Q9N1
Absorption
Active Site ACT_SITE 165; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 211; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 243; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7
Activity Regulation
Binding Site BINDING 95; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 166; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; BINDING 190; /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:0000305|PubMed:25910960};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000305|PubMed:25910960}; 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:25910960};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:25910960}; CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:25910960};
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:25910960). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:25910960). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25910960). Can also depolymerize the synthetic polyester poly(epsilon-caprolactone) (PCL) (PubMed:25910960). {ECO:0000269|PubMed:25910960}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:25910960};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:25910960};
Pathway
nucleotide Binding
Features Active site (3); Binding site (3); Chain (1); Disulfide bond (1); Mutagenesis (2); Region (1); Signal peptide (1)
Keywords Disulfide bond;Hydrolase;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..35; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 31,787
Kinetics
Metal Binding
Rhea ID RHEA:49528; RHEA:49529; RHEA:47348; RHEA:47349
Cross Reference Brenda 3.1.1.74;