Detail Information for IndEnz0002000563
IED ID IndEnz0002000563
Enzyme Type ID protease000563
Protein Name Aspergillopepsin-1
EC 3.4.23.18
Aspartic protease pepA
Aspergillopepsin I
Aspergillopeptidase A
Proctase B
Gene Name pepA prtB
Organism Aspergillus niger
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger
Enzyme Sequence MVVFSKTAALVLGLSTAVSAAPAPTRKGFTINQIARPANKTRTVNLPGLYARSLAKFGGTVPQSVKEAASKGSAVTTPQNNDEEYLTPVTVGKSTLHLDFDTGSADLWGFSDELPSSEQTGHDLYTPSSSATKLSGYSWDISYGDGSSASGDVYRDTVTVGGVTTNKQAVEAASKISSEFVQDTANDGLLGLAFSSINTVQPKAQTTFFDTVKSQLDSPLFAVQLKHDAPGVYDFGYIDDSKYTGSITYTDADSSQGYWGFSTDGYSIGDGSSSSSGFSAIADTGTTLILLDDEIVSAHYEQVSGAQESYEAGGYVFSCSTDLPDFTVVIGDYKAVVPGKYINYAPVSTGSSTCYGGIQSNSGLGLSILGDVFLKSQYVVFNSEGPKLGFAAQA
Enzyme Length 394
Uniprot Accession Number P55325
Absorption
Active Site ACT_SITE 101; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 283; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.; EC=3.4.23.18; Evidence={ECO:0000250|UniProtKB:Q12567};
DNA Binding
EC Number 3.4.23.18
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 also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A. {ECO:0000250|UniProtKB:Q12567}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (1); Domain (1); Propeptide (1); Sequence conflict (11); Signal peptide (1)
Keywords Aspartyl protease;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
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 41,230
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda