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Carboxypeptidase G from Pseudomonas sp., or γ-Glutamyl hydrolase, has been used in a study to assess the role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations. Carboxypeptidase G from Pseudomonas sp. has also been used in a study to investigate the effects of nitric oxide on pemetrexed cytotoxicity via NO?cGMP signaling in lung adenocarcinoma cells.

Carboxypeptidase G is a lysosomal, thiol-dependent protease, which progressively cleaves γ-glutamyl pteroyl poly-γ-glutamate yielding pteroyl-α-glutamate (folic acid) and free glutamate. It is considered highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid of the leaving group. Molecular mass of this homodimer is approximately 90 kDa. The enzyme is activated by Zn2+ ions.