Detail Information for IndEnz0002004489
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