EC Number   |
Application |
Reference |
|---|
   3.4.17.11 | diagnostics |
the enzyme is used in targeted cancer strategies such as antibody-directed enzyme prodrug therapy |
752914 |
| 3.4.17.11 | drug development |
enzyme is used in enzyme prodrug therapy to treat human breast cancer, the enzyme catalyzes the activation of the di- and trifluorinated prodrugs |
-, 669785 |
| 3.4.17.11 | medicine |
carboxypeptidase G2 is a bacterial enzyme that is currently employed in a range of targeted cancer chemotherapy strategies such as gene-directed enzyme prodrug therapy (GDEPT). These therapeutic strategies would benefit from robust imaging strategies that afford high spatial and temporal resolution images of the biodistribution of carboxypeptidase G2 activity. Employing dynamic nuclear polarization (DNP) and natural abundance 13C magnetic resonance spectroscopy (MRS), the carboxypeptidase G2-mediated conversion of a novel hyperpolarized reporter probe 3,5-difluorobenzoyl-L-glutamic acid to 3,5-difluorobenzoic acid and L-glutamic acid is observed in vitro. The potential for translation in vivo will primarily depend on the 13C relaxation times and this appears to be an important limiting factor in the case of 3,5-difluorobenzoyl-L-glutamic acid |
709782 |
| 3.4.17.11 | medicine |
CPG2 possesses several properties that make it suitable for suicide gene therapy |
697374, 700491 |
| 3.4.17.11 | medicine |
design of a series of circular permutations of the medically important enzyme, carboxypeptidase G2, that show similar structure and stability to the wild-type, while retaining equivalent enzymatic activity in most cases. One of the circular permutants confers methotrexate resistance when expressed in Escherichia coli similarly to wild-type carboxypeptidase G2. The circular permutants provide a promising starting point for generating a protease regulatable form of carboxypeptidase G2, which will be valuable in advancing directed enzyme-prodrug chemotherapy technology |
755292 |
| 3.4.17.11 | medicine |
enzyme is used in enzyme prodrug therapy to treat human breast cancer, the enzyme catalyzes the activation of the di- and trifluorinated prodrugs |
-, 669785 |
| 3.4.17.11 | medicine |
glutamate carboxypeptidase inhibition is evident for a neuroprotective role in several chronic models of chemotherapy-induced peripheral neuropathy and claims an approach for the clinical treatment of this pathology |
710122 |
| 3.4.17.11 | medicine |
glutamate chemical exchange saturation transfer magnetic resonance imaging GluCEST-MRI is an attractive method for metabolic imaging of glutamate. The change in glutamate concentration measured with GluCEST MRI could provide a noninvasive biomarker of carboxypeptidase G2 activity, in addition to acting as a surrogate for prodrug activation and the concentration of activated drug in the tumor |
732516 |
| 3.4.17.11 | medicine |
potential use in antibody directed enzyme prodrug therapy (ADEPT) |
679268, 681100 |
| 3.4.17.11 | medicine |
side effects of methotrexate especially hepatotoxicity limits clinical applications of this anticancer agent. Carboxypeptidase G2 fused to the transactivator transduction domain (TAT) is administrated for the treatment of elevated plasma concentrations of methotrexate. TAT-CPG2 significantly prevents methotrexate-induced oxidative stress by decreasing the formation of reactive oxygen species (ROS) and increasing the content of glutathione (GSH) and catalase activity. Both native and denatured TAT-carboxypeptidase G2 strongly protect HepG2 cells against methotrexate-induced oxidative stress and apoptosis. Intracellular delivery of carboxypeptidase G2 might provide a new therapeutic strategy for protecting against methotrexate mediated cytotoxicity |
755593 |
