>> -Asp . Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -GluAsp- and -GluPro- bonds is slow
Reaction: Preferential cleavage: -Glu >> -Asp . Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -GluAsp- and -GluPro- bonds is slow
Other names: GluSGP
Comments: From Streptomyces griseus. A peptidase of family S1 (trypsin family). Inhibited by [Leu18→Glu]-modified turkey ovomucoid third domain
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 137010-42-5
References
1. Yoshida, N., Tsuruyama, S., Nagata, K., Hirayama, K., Noda, K. and Makisumi, S. Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase). J. Biochem. (Tokyo) 104 (1988) 451-456. [PMID: 3149277]
2. Komiyama, T., Bigler, T.L., Yoshida, N., Noda, K. and Laskowski, M., Jr Replacement of P1 Leu18 by Glu18 in the reactive site of turkey ovomucoid third domain converts it into a strong inhibitor of Glu-specific Streptomyces griseus Proteinase (GluSGP). J. Biol. Chem. 266 (1991) 10727-10730. [PMID: 1674942]
3. Nagata, K., Yoshida, N., Ogata, F., Araki, M. and Noda, K. Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8. J. Biochem. (Tokyo) 110 (1991) 859-862. [PMID: 1794975]
4. Svendsen, I., Jensen, M.R. and Breddam, K. The primary structure of the glutamic acid-specific protease of Streptomyces griseus. FEBS Lett. 292 (1991) 165-167. [PMID: 1959600]
5. Breddam, K. and Meldal, M. Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biochem. 206 (1992) 103-107. [PMID: 1587264]