| IED ID | IndEnz0010001200 |
| Enzyme Type ID | esterase001200 |
| Protein Name |
Cutinase cut1 EC 3.1.1.74 Thcut1 |
| Gene Name | cut1 |
| Organism | Trichoderma harzianum (Hypocrea lixii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Trichoderma harzianum (Hypocrea lixii) |
| Enzyme Sequence | MRSLSLFTALLAGQAFAYPKPVLQSSTRRDWPTINEFLTELAEIMPIGDTVSAACDLIGDAEDVAADLFDISNTENDACGDVTVLFARGTCDPGNVGVLVGPWFFNSLETALPNKKVGVKGVPYPASVQGFLSGSVQPGIDMANQIKSVISSCPNTKLVLGGYSQGSMVVHNAASNLDAATMAKVSAVVLFGDPYDGRPVANYDASKVLVVCHDGDNICQGGDFILLPHLTYAEDADTAAAFVKPLVS |
| Enzyme Length | 248 |
| Uniprot Accession Number | A8QPD8 |
| Absorption | |
| Active Site | ACT_SITE 164; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 216; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 229; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00590 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:18987860}; |
| DNA Binding | |
| EC Number | 3.1.1.74 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18987860). May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18987860). May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues (PubMed:18987860). {ECO:0000269|PubMed:18987860}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8. {ECO:0000269|PubMed:18987860}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1); Site (2) |
| Keywords | Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Induced during growth on olive oil (PubMed:18987860). Induced during growth on the lipidic carbon source 16-hydroxyhexadecanoic acid (synthetic cutin monomer) (PubMed:18987860). Induced during growth on plant material (PubMed:18987860). Induced during growth on pectin (PubMed:18987860). Repressed during growth on glucose carbon source (PubMed:18987860). {ECO:0000269|PubMed:18987860}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18987860}. |
| Modified Residue | |
| Post Translational Modification | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255|RuleBase:RU361263 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,007 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 mM for p-nitrophenyl acetate (at pH 8 and 25 degrees Celsius) {ECO:0000269|PubMed:18987860}; KM=0.57 mM for p-nitrophenyl butyrate (at pH 8 and 25 degrees Celsius) {ECO:0000269|PubMed:18987860}; KM=0.82 mM for p-nitrophenyl valerate (at pH 8 and 25 degrees Celsius) {ECO:0000269|PubMed:18987860}; KM=0.085 mM for p-nitrophenyl palmitate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:18987860}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |