Aspergillopepsin I

Aspergillopepsin I
Identifiers
EC number 3.4.23.18
CAS number 9025-49-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Aspergillopepsin I (EC 3.4.23.18, Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus awamori acid proteinase, Aspergillus carboxyl proteinase, 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) is an enzyme.[1][2][3][4][5][6][7][8][9][10] This enzyme catalyses the following chemical 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

This enzyme is found in a variety of Aspergillus species.

See also

References

  1. ↑ Kovaleva, G.G.; Shimanskaya, M.P.; Stepanov, V.M. (1972). "The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergillus awamori - an analog of penicillopepsin and pepsin". Biochem. Biophys. Res. Commun. 49: 1075–1082. doi:10.1016/0006-291x(72)90322-1. PMID 4565799.
  2. ↑ Morihara, K.; Oka, T. (1973). "Comparative specificity of microbial acid proteinases for synthetic peptides. III. Relationship with their trypsinogen activating ability". Arch. Biochem. Biophys. 157: 561–572. doi:10.1016/0003-9861(73)90675-9. PMID 4581238.
  3. ↑ Davidson, R.; Gertler, A.; Hofmann, T. (1975). "Aspergillus oryzae' acid proteinase. Purification and properties, and formation of π-chymotrypsin". Biochem. J. 147: 45–53. PMID 239702.
  4. ↑ Chang, W.-J.; Horiuchi, S.; Takahashi, K.; Yamasaki, M.; Yamada, Y. (1976). "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: 975–981. PMID 12156.
  5. ↑ Tanaka, N.; Takeuchi, M.; Ichishima, E. (1977). "Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity". Biochim. Biophys. Acta. 485: 406–416. doi:10.1016/0005-2744(77)90176-0. PMID 21699.
  6. ↑ Ostoslavskaya, V.I.; Kotlova, E.K.; Stepanov, V.M.; Rudenskaya, G.H.; Baratova, L.A.; Belyanova, L.P. (1976). "Aspergillopepsin F-A carboxylic proteinase from Aspergillus foetidus". Bioorg. Khim. 5: 595–603.
  7. ↑ Panneerselvam, M.; Dhar, S.C. (1981). "Studies on the peptide bond specificity and the essential groups of an acid proteinase from Aspergillus fumigatus". Ital. J. Biochem. 30: 207–216. PMID 7024192.
  8. ↑ Ostoslavskaya, V.I.; Revina, L.P.; Kotlova, E.K.; Surova, I.A.; Levin, E.D.; Timokhima, E.A.; Stepanov, V.M. (1986). "The primary structure of aspergillopepsin A, aspartic proteinase from Aspergillus awamori. IV. Amino acid sequence of the enzyme". Bioorg. Khim. 12: 1030–1047.
  9. ↑ Yagi, F.; Fan, J.; Tadera, K.; Kobayashi, A. (1986). "Purification and characterization of carboxyl proteinase from Aspergillus kawachii". Agric. Biol. Chem. 50: 1029–1033. doi:10.1271/bbb1961.50.1029.
  10. ↑ Majima, E.; Oda, K.; Murao, S.; Ichishima, E. (1988). "Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate". Agric. Biol. Chem. 52: 787–793. doi:10.1271/bbb1961.52.787.

External links

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