Acting on peptide bonds (peptidases);
Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen
Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The two species variants show 83% sequence identity and are immunologically crossreactive. In peptidase family A1 (pepsin A family). Formerly included in EC 22.214.171.124
EC 126.96.36.199 created 1992 (EC 188.8.131.52 created 1992 (EC 184.108.40.206 created 1961 as EC 220.127.116.11, transferred 1972 to EC 18.104.22.168, modified 1981 [EC 22.214.171.124, EC 126.96.36.199, EC 188.8.131.52, EC 184.108.40.206, EC 220.127.116.11, EC 18.104.22.168 and EC 22.214.171.124 all created 1972 and incorporated 1978], part incorporated 1992)
Baudys M, Foundling S, Pavlik M, Blundell T, Kostka V
Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment.