ExplorEnz: EC 3.4.21.82

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3.4.21.82

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

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, 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. [DOI] [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. [DOI] [PMID: 1587264]

[EC 3.4.21.82 created 1993]