| IED ID | IndEnz0010001089 |
| Enzyme Type ID | esterase001089 |
| Protein Name |
Cutinase 1 EC 3.1.1.74 Cutin hydrolase 1 L1 |
| Gene Name | cutL CutL1 AO090005000029 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MHLRNIVIALAATAVASPVDLQDRQLTGGDELRDGPCKPITFIFARASTEPGLLGISTGPAVCNRLKLARSGDVACQGVGPRYTADLPSNALPEGTSQAAIAEAQGLFEQAVSKCPDTQIVAGGYSQGTAVMNGAIKRLSADVQDKIKGVVLFGYTRNAQERGQIANFPKDKVKVYCAVGDLVCLGTLIVAPPHFSYLSDTGDASDFLLSQLG |
| Enzyme Length | 213 |
| Uniprot Accession Number | P52956 |
| Absorption | |
| Active Site | ACT_SITE 126; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:19810726, ECO:0007744|PDB:3GBS"; ACT_SITE 181; /evidence="ECO:0000269|PubMed:19810726, ECO:0007744|PDB:3GBS"; ACT_SITE 194; /note="Proton donor/acceptor"; /evidence="ECO:0000269|PubMed:19810726, ECO:0007744|PDB:3GBS" |
| Activity Regulation | ACTIVITY REGULATION: Competitively inhibited by the carboxylic acids butyric acid, valeric acid and hexanoic acid (PubMed:15968570). Competitively inhibited by the dicarboxylic acid succinic acid (PubMed:15968570). Competitively inhibited by the alcohols propan-1-ol, butan-1-ol, hexan-1-ol, octan-1-ol, and butane-1,4-diol (PubMed:15968570). {ECO:0000269|PubMed:15968570}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000305|PubMed:15968570, ECO:0000305|PubMed:19810726}; |
| 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:19810726, PubMed:15968570). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:19810726, PubMed:15968570). {ECO:0000269|PubMed:15968570, ECO:0000269|PubMed:19810726}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-40 degrees Celsius (PubMed:19810726). Optimum temperature is 35-55 degrees Celsius (PubMed:15968570). {ECO:0000269|PubMed:15968570, ECO:0000269|PubMed:19810726}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:15968570}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (6); Chain (1); Disulfide bond (3); Helix (11); Signal peptide (1); Site (2); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3GBS; 3QPD; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,263 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.96 uM for p-nitrophenyl acetate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=1100 uM for p-nitrophenyl propionate (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:15968570}; KM=0.21 uM for p-nitrophenyl butyrate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=220 uM for p-nitrophenyl butyrate (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:15968570}; KM=0.04 uM for p-nitrophenyl valerate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=44 uM for p-nitrophenyl valerate (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:15968570}; KM=0.29 uM for p-nitrophenyl hexanoate (at pH 7.5) {ECO:0000269|PubMed:19810726}; Note=kcat is 11 sec(-1) with p-nitrophenyl propionate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 18 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 14 sec(-1) with p-nitrophenyl valerate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). {ECO:0000269|PubMed:15968570}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |