| IED ID | IndEnz0010000317 |
| Enzyme Type ID | esterase000317 |
| Protein Name |
Cutinase EC 3.1.1.74 |
| Gene Name | M419DRAFT_76732 |
| Organism | Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
| Enzyme Sequence | MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS |
| Enzyme Length | 248 |
| Uniprot Accession Number | A0A024SC78 |
| Absorption | |
| Active Site | ACT_SITE 164; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:25219509, ECO:0007744|PDB:4PSE"; ACT_SITE 216; /evidence="ECO:0000250|UniProtKB:P00590"; ACT_SITE 229; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P00590" |
| Activity Regulation | ACTIVITY REGULATION: Weakly inhibited by n-undecyl phosphonate (C11Y4) (PubMed:25219509). Activity unaffected by paraoxon (PubMed:25219509). {ECO:0000269|PubMed:25219509}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:25219509}; |
| 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:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Propeptide (1); Region (1); Signal peptide (1); Site (2) |
| Keywords | 3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}. |
| 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 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 4PSC; 4PSD; 4PSE; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,924 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |