Protease, Staph aureus (Endoproteinase Glu-C)
Enzymatic Reaction (image will open in a new window)
Protease S. aureus, V8 (endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids (Drapeau et al. 1972). Houmard and Drapeau (1972) report that in the presence of ammonium buffers the enzyme specificity can be limited to glutamoyl bonds. Its rather unique specificity, which can be considered as opposite to that of trypsin, makes it a useful tool for protein chemistry and peptide mapping studies (Cleveland et al. 1977) and (Hall et al. 1978).
Characteristics of Protease from S. aureus, V8:
Molecular weight: 27,000 (Drapeau 1978).
Extinction coefficient: = 4.26 (Houmard 1976).
Optimum pH: 4.0 and 7.8 with hemoglobin substrate. (Drapeau et al. 1972).
Inhibitors: Diisopropyl fluorophosphate (DFP) and monovalent anions such as F-, Cl-, Br-, CH3COO-, and NO3- (Houmard 1976).