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Literature summary for 1.4.1.27 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
Search for more literature for 1.4.1.27

Inhibitors

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

KM Value [mM]

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

Organism

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

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
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Substrates and Products (Substrate)

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

General Information

General Information Comment Organism
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