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

BRENDA support

Literature summary for 6.3.4.14 extracted from

  • Monnot, S.; Serre, V.; Chadefaux-Vekemans, B.; Aupetit, J.; Romano, S.; De Lonlay, P.; Rival, J.M.; Munnich, A.; Steffann, J.; Bonnefont, J.P.
    Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency (2009), Hum. Mutat., 30, 734-740.
    View publication on PubMed
Search for more literature for 6.3.4.14

Application

Application Comment Organism
medicine identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 component of pyruvate carboxylase
-