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
-
diagnostics
-
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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Cloned
Cloned on EC 3.4.17.11 - glutamate carboxypeptidase
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high-yield expression in Escherichia coli, expression of the full-length enzyme, as well as protein fragments corresponding to the individual catalytic and dimerization domains
into a binary vector for Agrobacterium tumefaciens-mediated transformation
overexpression of a codon-optimized gene in Escherichia coli, vector pET28a, the enzyme is expressed to about 60% of the total host protein and the purification of the recombinant His-tagged protein could be achieved in a single step by Ni2+ charged column chromatography