Rhizopuspepsin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.21 Rhizopuspepsin
Rhizopuspepsin is an aspartic endopeptidase from the zygomycete Rhizopus chinensis, with a similar enzyme in R. niveus, belonging to peptidase family A1. Like pepsin A it hydrolyzes proteins broadly, favoring hydrophobic residues at P1 and P1', clots milk and activates trypsinogen; it does not cleave Gln4-His but does cleave His10-/-Leu and Val12-/-Glu in the insulin B chain. In the fungus it digests extracellular proteins. It features a pepsin-like aspartic-protease fold.
Rhizopuspepsin is an aspartic endopeptidase from the zygomycete Rhizopus chinensis, with a similar enzyme in R. niveus, belonging to peptidase family A1. Like pepsin A it hydrolyzes proteins broadly, favoring hydrophobic residues at P1 and P1', clots milk and activates trypsinogen; it does not cleave Gln4-His but does cleave His10-/-Leu and Val12-/-Glu in the insulin B chain. In the fungus it digests extracellular proteins. It features a pepsin-like aspartic-protease fold.
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