3.4.17.11: glutamate carboxypeptidase
This is an abbreviated version!
For detailed information about glutamate carboxypeptidase, go to the full flat file.
Word Map on EC 3.4.17.11
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3.4.17.11
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methotrexate
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prodrugs
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high-dose
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antibody-directed
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leucovorin
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hdmtx
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methotrexate-induced
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gene-directed
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naaladase
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gdept
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antibody-enzyme
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medicine
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anti-cea
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anti-carcinoembryonic
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prodrug-activating
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gcpii
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2-pmpa
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n-acetyl-aspartyl-glutamate
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dampa
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drug development
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diagnostics
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pharmacology
- 3.4.17.11
- methotrexate
-
prodrugs
-
high-dose
-
antibody-directed
- leucovorin
-
hdmtx
-
methotrexate-induced
-
gene-directed
- naaladase
-
gdept
-
antibody-enzyme
- medicine
-
anti-cea
-
anti-carcinoembryonic
-
prodrug-activating
- gcpii
- 2-pmpa
-
n-acetyl-aspartyl-glutamate
-
dampa
- drug development
- diagnostics
- pharmacology
Reaction
release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups =
Synonyms
carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, CPDG2, CPG2, folate hydrolase G2, glucarpidase, glutamate carboxypeptidase, glutamyl carboxypeptidase, N-pteroyl-L-glutamate hydrolase, pteroylmonoglutamic acid hydrolase G2
ECTree
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Application on EC 3.4.17.11 - glutamate carboxypeptidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diagnostics
the enzyme is used in targeted cancer strategies such as antibody-directed enzyme prodrug therapy
drug development
medicine
pharmacology
the enzyme is used in antibody directed enzyme prodrug therapy to catalyse the formation of an active drug from an inert prodrug. Free carboxypeptidase G2 in the bloodstream must be inhibited before administration of the prodrug in order to avoid a systemic reaction in the patient
drug development
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enzyme is used in enzyme prodrug therapy to treat human breast cancer, the enzyme catalyzes the activation of the di- and trifluorinated prodrugs
drug development
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enzyme is used in enzyme prodrug therapy to treat human breast cancer, the enzyme catalyzes the activation of the di- and trifluorinated prodrugs
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medicine
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enzyme is used in enzyme prodrug therapy to treat human breast cancer, the enzyme catalyzes the activation of the di- and trifluorinated prodrugs
medicine
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the enzyme is used in antibody-directed enzyme prodrug therapy, ADEPT, e.g. against colorectal carcinoma expressing carcinoembryonic antigen, overview
medicine
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potential use in antibody directed enzyme prodrug therapy (ADEPT)
medicine
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CPG2 possesses several properties that make it suitable for suicide gene therapy
medicine
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CPG2 possesses several properties that make it suitable for suicide gene therapy
medicine
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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
medicine
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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
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
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
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
medicine
the enzyme is used in drug detoxification when cancer patients have excessive levels of the anti-cancer agent methotrexate
medicine
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enzyme is used in enzyme prodrug therapy to treat human breast cancer, the enzyme catalyzes the activation of the di- and trifluorinated prodrugs
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