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 (Comment) | Organism |
---|---|
modeling of three-dimensional structure | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |