EC Number   |
Application |
Reference |
|---|
    1.4.1.27 | medicine |
in 14 patients from 13 families with clinical and biochemical features suggestive of glycine encephalopathy, mutations of the glycine cleavage system are identified. Seven patients (50%) have biallelic mutations in GldC gene, six patients (43%) have biallelic mutations in Amt gene and one patient (7%) has mutation identified in only one allele in GldC gene. Majority of the mutations in GldC and AMT are missense mutations and family-specific. No mutation is found in GcsH gene |
743023 |
| 1.4.1.27 | 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 |
759767 |
| 1.4.1.27 | synthesis |
recombinant expression of H-protein in Escherichia coli. When the cells are cultured in medium supplemented with 30 microM lipoate, about 10% of the protein expressed is the correctly lipoylated active form, 10% is an inactive aberrantly modified form, and the remaining 80% is the unlipoylated apoform |
759452 |
