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Literature summary for 6.4.1.1 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

Application

Application Comment Organism
medicine identification of mutations of the pyruvate carboxylase gene, in five unrelated patients. Pyruvate deficiency form B is consistently associated with at least one truncating mutation, mostly lying in the C-terminal part of carboxyltransferase or BCCP domains, whereas form A always results from association of two missense mutations located in biotin carboxylase or N-terminal part of carboxyltransferase domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the newly identified pyruvate carboxylase-deficient patients is biotin-responsive Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of three-dimensional structure Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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