| IED ID | IndEnz0002019032 |
| Enzyme Type ID | protease019032 |
| Protein Name |
Ervatamin-C ERV-C EC 3.4.22.- |
| Gene Name | |
| Organism | Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Gentianales Apocynaceae Rauvolfioideae Tabernaemontaneae Tabernaemontaninae Tabernaemontana Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
| Enzyme Sequence | LPEQIDWRKKGAVTPVKNQGSCGSCWAFSTVSTVESINQIRTGNLISLSEQELVDCDKKNHGCLGGAFVFAYQYIINNGGIDTQANYPYKAVQGPCQAASKVVSIDGYNGVPFCNEXALKQAVAVQPSTVAIDASSAQFQQYSSGIFSGPCGTKLNHGVTIVGYQANYWIVRNSWGRYWGEKGYIRMLRVGGCGLCGIARLPYYPTKA |
| Enzyme Length | 208 |
| Uniprot Accession Number | P83654 |
| Absorption | |
| Active Site | ACT_SITE 25; /evidence=ECO:0000250|UniProtKB:P00785; ACT_SITE 157; /evidence=ECO:0000250|UniProtKB:P00785; ACT_SITE 173; /evidence=ECO:0000250|UniProtKB:P00785 |
| Activity Regulation | ACTIVITY REGULATION: Activated by thio-specific activators such as cysteine, beta-mercaptoethanol, DTT and glutathione. Inhibited by the thiol-specific inhibitors leupeptin, iodoacetamide, PCMB, NEM, mercuric chloride and sodium tetrathionate. {ECO:0000269|PubMed:9836431}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Cysteine proteinase. Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity. Has little or no activity against synthetic substrates. {ECO:0000269|PubMed:9836431}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with azoalbumin as substrate. Thermostable up to 70 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0 with azoalbumin or hemoglobin as substrate. Active and stable from pH 2.0 to 12.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (8); Chain (1); Disulfide bond (4); Helix (7); Sequence conflict (2); Turn (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2, ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1O0E; 2PNS; |
| Mapped Pubmed ID | 17767923; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,523 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.09 uM for azoalbumin; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B50; |