ExplorEnz: EC 3.4.23.18

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3.4.23.18

Accepted name:

aspergillopepsin I

Reaction:

Hydrolysis of proteins with broad specificity. Generally favours hydrophobic residues in P1 and P1′, but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk

Other name(s):

Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase; Aspergillus niger acid proteinase; sumizyme AP; proctase P; denapsin; denapsin XP 271; proctase

Comments:

Found in a variety of Aspergillus species (imperfect fungi): Aspergillus awamori (awamorin, aspergillopepsin A: [8]), A. foetidus (aspergillopepsin F: [6]), A. fumigatus [7], A. kawachii [9], A. niger (proteinase B, proctase B: [2,4]), A. oryzae (trypsinogen kinase: [3,10]), A. saitoi (aspergillopeptidase A: [10]), and A. sojae [5,10]. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-49-4

References:

1.	Kovaleva, G.G., Shimanskaya, M.P. and Stepanov, V.M. The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergillus awamori - an analog of penicillopepsin and pepsin. Biochem. Biophys. Res. Commun. 49 (1972) 1075–1082. [DOI] [PMID: 4565799]
2.	Morihara, K. and Oka, T. Comparative specificity of microbial acid proteinases for synthetic peptides. III. Relationship with their trypsinogen activating ability. Arch. Biochem. Biophys. 157 (1973) 561–572. [PMID: 4593189]
3.	Davidson, R., Gertler, A. and Hofmann, T. Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin. Biochem. J. 147 (1975) 45–53. [PMID: 239702]
4.	Chang, W.-J., Horiuchi, S., Takahashi, K., Yamasaki, M. and Yamada, Y. The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus. J. Biochem. (Tokyo) 80 (1976) 975–981. [PMID: 12156]
5.	Tanaka, N., Takeuchi, M. and Ichishima, E. Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity. Biochim. Biophys. Acta 485 (1977) 406–416. [DOI] [PMID: 21699]
6.	Ostoslavskaya, V.I., Kotlova, E.K., Stepanov, V.M., Rudenskaya, G.H., Baratova, L.A. and Belyanova, L.P. Aspergillopepsin F-A carboxylic proteinase from Aspergillus foetidus. Bioorg. Khim. 5 (1976) 595–603.
7.	Panneerselvam, M. and Dhar, S.C. Studies on the peptide bond specificity and the essential groups of an acid proteinase from Aspergillus fumigatus. Ital. J. Biochem. 30 (1981) 207–216. [PMID: 7024192]
8.	Ostoslavskaya, V.I., Revina, L.P., Kotlova, E.K., Surova, I.A., Levin, E.D., Timokhima, E.A. and Stepanov, V.M. The primary structure of aspergillopepsin A, aspartic proteinase from Aspergillus awamori. IV. Amino acid sequence of the enzyme. Bioorg. Khim. 12 (1986) 1030–1047.
9.	Yagi, F., Fan, J., Tadera, K. and Kobayashi, A. Purification and characterization of carboxyl proteinase from Aspergillus kawachii. Agric. Biol. Chem. 50 (1986) 1029–1033.
10.	Majima, E., Oda, K., Murao, S. and Ichishima, E. Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate. Agric. Biol. Chem. 52 (1988) 787–793.

[EC 3.4.23.18 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992)]