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Literature summary extracted from

  • Kochi, H.; Seino, H.; Ono, K.
    Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes (1986), Arch. Biochem. Biophys., 249, 263-272 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.27 2-oxo-3-methylvalerate competitive with respect to glycine, presence leads to a decrease of apparent Km for NAD with a concomitant decrease of Vmax Rattus norvegicus
1.4.1.27 2-oxoglutarate competitive with respect to glycine, presence leads to a decrease of apparent Km for NAD with a concomitant decrease of Vmax Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.1.27 mitochondrion
-
 Rattus norvegicus 5739
-

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.27 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.27 liver
-
 Rattus norvegicus
-

General Information

EC Number General Information Comment Organism
1.4.1.27 physiological function the lipoamide dehydrogenase component, cf. EC 1.8.1.4, is an indistinguishable constituent among alpha-keto acid dehydrogenase complexes and the glycine cleavage system in mitochondria in nature, and lipoamide dehydrogenase-mediated transfer of reducing equivalents might regulate alpha-keto acid oxidation as well as glycine oxidation Rattus norvegicus