Glutamate endopeptidase

Momordica charantia (bitter gourd) (Cucurbitaceae) [seed] BGIA (68 aa 7 kDa 2 Cys 1 S-S) Streptomyces griseus Glutamate Endopeptidase [70 nM], Subtilisin Carlsberg [465]... 

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. 

Some other peptides, e.g., dipeptidyl peptidase IV (8), endopeptidase 3.4.24.16 inhibitor (9), and a copolymer of tyrosine, glutamic acid, alanine, and lysine (10), have also demonstrated immunomodulatory activity. Thus analogues of these may some day play an important role in treatment of autoimmune and inflammatory diseases. It should also be noted that a vast number of naturally derived peptides also has demonstrated antimicrobial activity toward a wide range of pathogens (11), resulting in possible templates for further optimization studies clearly demonstrating the potential importance of peptides as pharmacological tools. 

Park, O. and Allen, J.C. 1998. Preparation of phosphopeptides derived from as-casein and (3-casein using immobilized glutamic acid-specific endopeptidase and characterization of their calcium binding. J. Dairy Sci. 81, 2858-2865. 

V8 protease, EC 3.4.21.19, Endoproteinase Glu-C, protease I, protease type XVII-B, an extracellular endopeptidase from the V8 strain of Staphylococcus aureus. It cleaves peptide bonds on the C-terminal side of glutamic acid and, to a lesser extent, of aspartic acid. The X-ray crystallographic structure of V8 protease was described in 2004 [G. R. Drapeau et al., J. Biol. Chem. 1972, 247, 6720 L. Prasad et al, Acfa Crystallogr. 2004, D60, 256]. 

Some endopeptidases are very specific in cleaving peptide bonds. For example, the Staphylococcus aureus V8 endopeptidase will break only that peptide bond whose carbonyl function has been contributed by glutamic acid (in other words the peptide bond must have a glutamic acid residue lying towards the amino terminal end) bovine pancreas elastase will break only those peptide bonds whose carbonyl function is contributed by alanine, glycine, serine, or valine. 

Wehofsky, N., Wissmarm, J., AUsch, M., Bordusa, F. (2000). Engineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases design, synthesis, and application. Biochim. Biophys. Acta, 1479,114-122. 

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