Carboxypeptidase G2 (CPG2) from Pseudomonas RS?16 is a 42 kDa exopeptidase in the aminoacylase?1/M20 family of enzymes that is not found in mammals.  Like other structurally related peptidases, the active conformation of CPG2 requires homodimerization and the presence of two atoms of zinc per subunit. Each subunit of the active enzyme contains a zinc-binding domain and a dimerization domain, both of which participate in catalysis.It has been exploited to cleave glutamic acid from a variety of prodrugs to release potent nitrogen mustards. CPG2 has great potential for ADEPT in model systems and in the clinic.


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