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Literature summary for 1.4.1.27 extracted from

  • Okamura-Ikeda, K.; Fujiwara, K.; Motokawa, Y.
    Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system (1982), J. Biol. Chem., 257, 135-139 .
    View publication on PubMed
Search for more literature for 1.4.1.27

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
 tetrahydrofolate pH 8.0, 37°C Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
 sedimentation equilibrium centrifugation, component T-protein Gallus gallus
38000
-
 gel filtration, component T-protein Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus P28337 i.e. aminomethyltransferase component T-protein, cf. EC 2.1.2.10
-

Purification (Commentary)

Purification (Comment) Organism
isolation of component T-protein Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
multimer x * 41000, SDS-PAGE, component T-protein Gallus gallus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Gallus gallus
tetrahydrofolate
-
 Gallus gallus

pI Value

Organism Comment pI Value Maximum pI Value
Gallus gallus component T-protein
-
 9.8

General Information

General Information Comment Organism
physiological function the component T-protein catalyzes the degradation of the protein-bound intermediate (-CH2NH2 moiety of glycine) to a 1-carbon unit and NH3. The reaction is dependent on tetrahydrofolate. T-protein associates with H-protein forming a complex of one molecule each of T-protein and H-protein Gallus gallus