Detail Information for IndEnz0002000083
IED ID IndEnz0002000083
Enzyme Type ID protease000083
Protein Name Penicillopepsin-1
EC 3.4.23.20
Aspartic protease pepA
Gene Name pepA TSTA_012870
Organism Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces stipitatus Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Enzyme Sequence MVNSKTVVSALALSALAAAAPAPSSTTSFSINQVAVKKPAIHPAVKYAKALAKYHAEIPSNVASAAASAQSGSATNKPTADDEEYVTPITAGSSTLHLDFDTGSADLWTYSASTRGVGSHSTYDTSTGKKVSGASWQISYGDGSSASGVVYKDKVVVGGVTASSQAVEVATQVSSEFSQDTSNDGLLGLAFSSINTVSPTPQKTFYDNVKSSLAKPVFAVTLKHQAPGTYDFGFIDKSKYKGSLAYTNVDNSQGFWQFTADGYSIGGSGGGSSFSAIADTGTTLVLLDDSIVDEYYSQVQGAQNDSSQGGYVFDCSADLPDFGVQIGDYTAVIPGKYINYASTGSTCFGGIQSNSGIGFSILGDVFLKSQYVVFDGDNLQLGFAAQA
Enzyme Length 387
Uniprot Accession Number B8MF81
Absorption
Active Site ACT_SITE 101; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 279; /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); Glycosylation (1); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01972}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 39,923
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda