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Literature summary extracted from

  • Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y.
    Mechanism of the glycine cleavage reaction. Further characterization of the intermediate attached to H-protein and of the reaction catalyzed by T-protein (1984), J. Biol. Chem., 259, 10664-10668 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.27 N-ethylmaleimide the modification of the free lipoyl sulfhydryl group renders the intermediate complex inactive Gallus gallus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.27 0.05
-
 tetrahydrofolate pH 8.0, 37°C Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.27 Gallus gallus P15505 i.e. component P-protein, glycine dehydrogenase, cf. EC 1.4.4.2
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.27 liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.27 glycine + tetrahydrofolate + NAD+
-
 Gallus gallus 5,10-methylenetetrahydrofolate + NH3 + CO2 + NADH
-
 ?

General Information

EC Number General Information Comment Organism
1.4.1.27 metabolism the amino group of glycine is retained in the intermediate and released as ammonia in the second partial reaction catalyzed by T-protein. The formation of ammonia accompanies the stoichiometric formation of 5,10-methylenetetrahydrofolate from the methylene carbon of glycine and tetrahydrofolate. The reaction proceeds through a sequential mechanism. Km values for the intermediate complex and tetrahydrofolate are 2.2 and 50 microM, respectively. In the absence of tetrahydrofolate, T-protein catalyzes the stoichiometric formation of ammonia and formaldehyde from the intermediate although the velocity is extremely low. The addition of tetrahydrofolate increases the rate about 2400fold Gallus gallus