| IED ID | IndEnz0010001303 |
| Enzyme Type ID | esterase001303 |
| Protein Name |
Cutinase 2 EC 3.1.1.74 Ancut2 Cutin hydrolase 2 |
| Gene Name | cut2 AN7541 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MHFKLLSLAALAGLSVASPLNLDERQLGSSSGNDLRDGDCKPVTFIFARASTEPGLLGMSTGPAVCNDLKADASLGGVACQGVGPKYTAGLAENALPQGTSSAAINEAKELFELAASKCPDTRIVAGGYSQGTAVMHGAIPDLSDEIKDKIAGVVLFGDTRNKQDGGQIKNFPKDKIKIYCATGDLVCDGTLVVTAAHFTYVANTGEASKWLEQQLASMPASTSTSSSSSSSSSAPASQTSQSSGLSSWFSGLGN |
| Enzyme Length | 255 |
| Uniprot Accession Number | Q5AVY9 |
| Absorption | |
| Active Site | ACT_SITE 130; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 185; /evidence=ECO:0000250|UniProtKB:P00590; ACT_SITE 198; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00590 |
| Activity Regulation | ACTIVITY REGULATION: Partially inhibited by the serine protease inhibitor phenylmethanesulfonyl fluoride (PubMed:28124733). Inhibited by various ions, including copper, iron, sodium, potassium, magnesium and calcium (PubMed:28124733). Inhibited by the chelating agent EDTA (ethylenediaminetetraacetic acid) (PubMed:28124733). Inhibited by the surfactants sodium dodecyl sulfate and polysorbate 80 (PubMed:28124733). {ECO:0000269|PubMed:28124733}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:22238011, ECO:0000269|PubMed:28124733}; |
| 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:16844780, PubMed:22238011, PubMed:28124733). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:22238011, PubMed:28124733). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity). {ECO:0000250|UniProtKB:Q5B2C1, ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:22238011, ECO:0000269|PubMed:28124733}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:28124733}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9-10.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Erroneous gene model prediction (2); Region (1); Signal peptide (1); Site (2) |
| Keywords | Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Induced during growth on cutin, in a manner dependent on transcription factors FarA and FARB (PubMed:30863878). Induced during growth on olive oil (PubMed:30863878, PubMed:22238011). Not induced during growth on the lipidic carbon sources 16-hydroxyhexadecanoic acid and propyl ricinoleate (synthetic cutin monomers), or triacetin and triesterate (triglycerides) (PubMed:30863878). Repressed during growth on glucose and on starch (PubMed:30863878, PubMed:22238011). {ECO:0000269|PubMed:22238011, ECO:0000269|PubMed:30863878}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,074 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.88 mM for p-nitrophenyl acetate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:28124733}; Note=kcat is 242 sec(-1) with p-nitrophenyl acetate as substrate (at pH 9 and 37 degrees Celsius). {ECO:0000269|PubMed:28124733}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |