Detail Information for IndEnz0002000493
IED ID IndEnz0002000493
Enzyme Type ID protease000493
Protein Name Penicillopepsin-3
EC 3.4.23.20
Aspartic protease pepB
Propenicillopepsin-JT3
Gene Name pepB
Organism Penicillium janthinellum (Penicillium vitale)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium janthinellum (Penicillium vitale)
Enzyme Sequence MVSFTQLQLAFLGLSALGAAVPVTGTSEKKTFSLNQVKVAGTKTKNPAEHYANALRKYGAEVPSHVLAAAAATGSVTTSPTEFDSEYLTPIDVGGTTMNLDIDTGSSDLWVFSKELPSSETSGHAVYSPSSQSQLLNGYSWSISYGDGSSASGNVYLDYVTVGGVTASSQAVEAAETISSEFQQDPSDGLMGLAFSSINTVQPESQSTFFDNVQSNLASPVFCADLKYEAPGVYDFGFIDSSKHTGSVTYTPVDNSQGFWGFTASGYAVGSGSTVSTSISGIADTGTTLLLLPSSIVKKYYAQVKGSSNSATYGGYVFPCSATLPKFTVVINGYKAVIAAQYLNYSPVETGSSTCFGGIQSDTGIGFSIFGDIFLKSQYVVFDASGPRLGFAPQ
Enzyme Length 394
Uniprot Accession Number Q9HEZ3
Absorption
Active Site ACT_SITE 103; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 284; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103
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', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.; EC=3.4.23.20; Evidence={ECO:0000250|UniProtKB:P00798};
DNA Binding
EC Number 3.4.23.20
Enzyme Function FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'. {ECO:0000250|UniProtKB:P00798}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (1); Domain (1); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Disulfide bond;Hydrolase;Protease;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01972}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 41,107
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.23.20;