Glutamyl endopeptidase

Glutamyl endopeptidase [EC 3.4.21.19] (also known as staphylococcal serine proteinase, V8 proteinase, protease V8, and endoproteinase Glu-C), a member of the peptidase family S2B, catalyzes the hydrolysis of Asp-Xaa and Glu-Xaa peptide bonds. In appropriate buffers, the specificity of the bond cleavage is restricted to Glu-Xaa. Peptide bonds involving bulky side chains of hydrophobic aminoacyl residues are hydrolyzed at a lower rate. 

Glutamyl endopeptidase 11 [EC 3.4.21.82], also known as glutamic acid-specific protease, catalyzes the hydrolysis of peptide bonds, exhibiting a preference for Glu-Xaa bonds much more than for Asp-Xaa bonds. The enzyme has a preference for prolyl or leucyl residues at P2 and phenylalanyl at P3. Hydrolysis of Glu-Pro and Asp-Pro bonds is slow. This endopeptidase is a member of the peptidase family S2A. 

Glutamyl endopeptidase. Staphylococcal serine proteinase. V8 proteinase. Protease V8. Endoproteinase Glu-C. 3.4.21.19 Preferential cleavage Asp-I-Xaa, Glu-I-Xaa. 

T. C. Friedman, S. Wilk, The Effect of Inhibitors of Prolyl Endopeptidase and Pyro-glutamyl Pephde Hydrolase on TRH Degradation in Rat Serum , Biochem. Biophys. Res. Commun. 1985, 132, 787-794. 

Lex A repressor), S26 (signal peptidase I), S41 (TSP protease), and S44 (tricorn protease). All known members of clan SH (catalytic triad His, Ser, His) are endopeptidases from DNA viruses which are involved in virus prohead assembly. The clan includes only the family S21 (Cytomegalovirus assemblin). Clan TA with the catalytic residue Thr, Ser or Cys, and an a,(3,a,p sandwich fold includes a number of peptidases whose only proteolytic activity is self-activation. Important families of this clan are T1 (proteasome), and S42 (y-glutamyl transpeptidase). 

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