| IED ID | IndEnz0002010981 |
| Enzyme Type ID | protease010981 |
| Protein Name |
Ochratoxinase OTase EC 3.4.17.- Amidohydrolase 2 Amidase 2 Carboxypeptidase Am2 |
| Gene Name | Am2 An14g02080 |
| Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
| 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 niger Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
| Enzyme Sequence | MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL |
| Enzyme Length | 480 |
| Uniprot Accession Number | A2R2V4 |
| Absorption | |
| Active Site | ACT_SITE 246; /evidence=ECO:0000269|PubMed:24947135; ACT_SITE 378; /evidence=ECO:0000269|PubMed:24947135 |
| Activity Regulation | ACTIVITY REGULATION: The Zn(2+)-specific chelator 1,10-phenanthroline inhibits the enzyme activity. {ECO:0000269|PubMed:24947135}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135). {ECO:0000269|PubMed:24947135, ECO:0000269|PubMed:33647354}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6); Mutagenesis (3) |
| Keywords | 3D-structure;Carboxypeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 4C5Y; 4C60; 4C65; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,200 |
| Kinetics | |
| Metal Binding | METAL 111; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y"; METAL 113; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y"; METAL 246; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y"; METAL 246; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y"; METAL 287; /note="Zinc 2; via pros nitrogen"; /evidence="ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y"; METAL 307; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y" |
| Rhea ID | |
| Cross Reference Brenda |