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Literature summary for 1.4.4.2 extracted from

  • Hiraga, K.; Kikuchi, G.
    The mitochondrial glycine cleavage system: differential inhibition by divalent cations of glycine synthesis and glycine decarboxylation in the glycine-CO2 exchange (1982), J. Biochem., 92, 937-944.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Co2+ inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation Gallus gallus
Cu2+ inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation Gallus gallus
Fe2+ slight inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation Gallus gallus
Ni2+ inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation Gallus gallus
Zn2+ inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Gallus gallus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycine + lipoylprotein Gallus gallus lipoyl protein: H-protein, lipoamide can also act as acceptor S-aminomethyldihydrolipoylprotein + CO2
-
?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycine + lipoylprotein lipoyl protein: H-protein, lipoamide can also act as acceptor Gallus gallus S-aminomethyldihydrolipoylprotein + CO2
-
?