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Literature summary for 1.4.1.27 extracted from

  • Kikuchi, G.; Hiraga, K.
    The mitochondrial glycine cleavage system - Unique features of the glycine decarboxylation (1982), Mol. Cell. Biochem., 45, 137-149 .
    View publication on PubMed
Search for more literature for 1.4.1.27

Application

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

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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 Homo sapiens 5739
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Organism

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
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Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
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Synonyms

Synonyms Comment Organism
Amt
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 Homo sapiens
DLDH
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 Homo sapiens
GLDC
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate linked to component P-protein Homo sapiens