Accepted name: glutamyl endopeptidase II
Reaction: Preferential cleavage: -Glu┼ >> -Asp┼ . Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu┼Asp- and -Glu┼Pro- bonds is slow
Other name(s): GluSGP
Comments: From Streptomyces griseus. A peptidase of family S1 (trypsin family). Inhibited by [Leu18→Glu]-modified turkey ovomucoid third domain
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]
[EC created 1993]

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