|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: glutamyl endopeptidase II
Enzyme Commission Synonyms: GluSGP
Enzyme Commission Summary:
This enzyme catalyzes 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.
From Streptomyces griseus. A peptidase of family S1 (trypsin family). Inhibited by [Leu18→Glu]-modified turkey ovomucoid third domain
Breddam92: Breddam K, Meldal M (1992). "Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching." Eur J Biochem 206(1);103-7. PMID: 1587264
Komiyama91: Komiyama T, Bigler TL, Yoshida N, Noda K, Laskowski M (1991). "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(17);10727-30. PMID: 1674942
Nagata91: Nagata K, Yoshida N, Ogata F, Araki M, Noda K (1991). "Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8." J Biochem 110(6);859-62. PMID: 1794975
Yoshida88: Yoshida N, Tsuruyama S, Nagata K, Hirayama K, Noda K, Makisumi S (1988). "Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase)." J Biochem 104(3);451-6. PMID: 3149277
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