Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.19.9 extracted from

  • Baugh, C.M.; Stevens, J.C.; Krumdieck, C.L.
    Studies on gamma-glutamyl carboxypeptidase. I. The solid phase synthesis of analogs of polyglutamates of folic acid and their effects on human liver gamma-glutamyl carboxypeptidase (1970), Biochim. Biophys. Acta, 212, 116-125.
    View publication on PubMed
Search for more literature for 3.4.19.9

General Stability

General Stability Organism
2-mercaptoethanol is required for stabilization Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information progressively removes gamma-glutamyl residues at acidic pH from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free gamma-glutamic acid, highly specific for the gamma-glutamyl bond, but not for the C-terminal amino acid (leaving group), action on gamma-glutamyl bonds is independent of an N-terminal pteroyl moiety Homo sapiens ?
-
 ?
polyglutamylfolate + H2O the ability of the gamma polyglutamate and the inability of the alpha polyglutamate to serve as substrate confirm the requirement for a terminal gamma peptide bond Homo sapiens ?
-
 ?
polyglutamylfolate + H2O specificity towards analogs of pteroylglutamyl-gamma-glutamyl-gamma-glutamic acid Homo sapiens ?
-
 ?
polyglutamylfolate + H2O analogs of the general structure pteroylglutamyl-gamma-glutamyl-gamma-R serve as substrates, low degree of specificity with regard to the nature of the-R group Homo sapiens ?
-
 ?