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Literature summary for 1.4.1.27 extracted from

  • Hayasaka, K.; Kochi, H.; Hiraga, K.; Kikuchi, G.
    Purification and properties of glycine decarboxylase, a component of the glycine cleavage system, from rat liver mitochondria and immunochemical comparison of this enzyme from various sources (1980), J. Biochem., 88, 1193-1199 .
    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
additional information
-
 additional information Km value of the isolated P-protein for H-protein in 0.0074 mM, pH 6.2, 37°C Rattus norvegicus
6.6
-
 glycine pH 6.2, 37°C Rattus norvegicus

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
 gel filtration of isolated P-protein Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
isolation of P-protein Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
multimer 2 * 105000, SDS-PAGE, component P-protein which forms a dimer Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 exchange reaction of the carboxyl carbon of glycine with CO2 catalyzed by the purified P-protein Rattus norvegicus