Application | Comment | Organism |
---|---|---|
medicine | in a patient with nonketotic hyperglycinemia, the H-protein purified from the liver is devoid of functional lipoic acid. H-protein from the patient is able to stimulate the P-protein-catalyzed exchange of the carboxyl carbon of glycine and CO2, although to a limited extent. P-Protein is inactivated when incubated with glycine in the presence of H-protein, and the inactivation is completely prevented when bicarbonate is further added. The inactivation is accompanied by a spectral change of P-protein. The inactivation of P-protein seems to reflect the formation of a ternary complex of P-protein, H-protein and aminomethyl moiety of glycine through a Schiff base linkage of the H-protein-bound aminomethyl moiety with the pyridoxal phosphate of P-protein | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P23378 and P09622 and P48728 | P23378 i.e. GldC, component P-protein, cf. EC 1.4.4.2, P09622 i.e. DldH, component L-protein, cf. 1.8.1.4, P48728 i.e. Amt, component T-protein, cf. EC 2.1.2.10 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
Amt | - |
Homo sapiens |
DLDH | - |
Homo sapiens |
GLDC | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | linked to component P-protein | Homo sapiens |