IED ID | IndEnz0002004489 |
Enzyme Type ID | protease004489 |
Protein Name |
Rhizopuspepsin EC 3.4.23.21 Fragment |
Gene Name | |
Organism | Rhizopus azygosporus (Rhizopus microsporus var. azygosporus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Mucoromycota Mucoromycotina Mucoromycetes Mucorales (pin molds) Mucorineae Rhizopodaceae Rhizopus Rhizopus azygosporus (Rhizopus microsporus var. azygosporus) |
Enzyme Sequence | AGVGTVP |
Enzyme Length | 7 |
Uniprot Accession Number | C0HLM4 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.; EC=3.4.23.21; Evidence={ECO:0000269|PubMed:31219401}; |
DNA Binding | |
EC Number | 3.4.23.21 |
Enzyme Function | |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 45-50 degrees Celsius with hemoglobin as substrate. Loses 50% of its activity at 60 degrees Celsius. {ECO:0000269|PubMed:31219401}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 with hemoglobin as substrate. {ECO:0000269|PubMed:31219401}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Non-terminal residue (2) |
Keywords | Aspartyl protease;Direct protein sequencing;Hydrolase;Protease |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 600 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |