Description
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.1 Molecular mass of this homodimer is approximately 90 kDa. The enzyme is activated by Zn2+ ions.
Abbr
Carboxypeptidase G, Native (Pseudomonas sp.)
Alias
γ-Glutamyl hydrolase
Applications
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.
Form
lyophilized powder contains sodium acetate salt.
Enzyme Commission Number
EC 3.4.17.11
Activity
> 3 units/mg protein
Composition
Protein, ~70% biuret
Unit Definition
One unit will hydrolyze 1.0 μmole of L-glutamic acid from (+)amethopterin per min at pH 7.3 at 30°C.
Synonyms
γ-Glutamyl hydrolase; EC 3.4.17.11; 9074-87-7; glutamate carboxypeptidase; carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase
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