The Enzyme Database

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Accepted name: scytalidoglutamic peptidase
Reaction: Hydrolysis of proteins, with a strong preference for Phe or Tyr at position P1 and one of the smaller amino-acids at P1′ in the sequence - P3 - P2 - P1 ┼P1′- P2′- P3′-. Cleaves the Tyr26-Thr27 bond in the B chain of oxidized insulin, which is not cleaved by pepsin.
Other name(s): scytalidopepsin-B; SCP-B; SGP; scytalidocarboxylpeptidase-B
Comments: The enzyme, isolated from the fungus Scytalidium lignicola and found in several other fungi, has a low pH optimum, being most active at pH 2 with casein as substrate. It differs from the pepsins (EC and EC in being insensitive to inhibition by pepstatin. It also differs from mammalian pepsins in showing a preference for a positively charged residue (Lys or Arg) at the P3 position. In addition to the catalytic Glu residue, a Gln residue appears to play an important role in the hydrolytic mechanism. A member of peptidase family G01, the "eqolisin" family of glutamic peptidases (G01.0001).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kataoka, Y., Takada, K., Oyama, H., Tsunemi, M., James, M.N. and Oda, K. Catalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases. FEBS Lett. 579 (2005) 2991–2994. [DOI] [PMID: 15907842]
2.  Fujinaga, M., Cherney, M.M., Oyama, H., Oda, K. and James, M.N. The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum. Proc. Natl. Acad. Sci. USA 101 (2004) 3364–3369. [DOI] [PMID: 14993599]
3.  Pillai, B., Cherney, M.M., Hiraga, K., Takada, K., Oda, K. and James, M.N. Crystal structure of scytalidoglutamic peptidase with its first potent inhibitor provides insights into substrate specificity and catalysis. J. Mol. Biol. 365 (2007) 343–361. [DOI] [PMID: 17069854]
4.  Kondo, M.Y., Okamoto, D.N., Santos, J.A., Juliano, M.A., Oda, K., Pillai, B., James, M.N., Juliano, L. and Gouvea, I.E. Studies on the catalytic mechanism of a glutamic peptidase. J. Biol. Chem. 285 (2010) 21437–21445. [DOI] [PMID: 20442413]
[EC created 2023]

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