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Literature summary for 1.4.1.27 extracted from

  • Hiraga, K.; Kikuchi, G.
    The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria (1980), J. Biol. Chem., 255, 11664-11670 .
    View publication on PubMed
Search for more literature for 1.4.1.27

Activating Compound

Activating Compound Comment Organism Structure
lipoic acid both glycine decarboxylation and the glycine-CO2 exchange catalyzed by P-protein are stimulated 100fold or more by the addition of lipoic acid Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
40
-
 glycine value for the isolated P-protein, pH 6.6, 37°C Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Gallus gallus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 0.1 mM, 83% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) Gallus gallus
Cu2+ 0.1 mM, 100% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein). Of the two partial reactions, decarboxylation of glycine yielding the H-protein-bound aminomethyl moiety is not significantly affected, but carboxylation of the H-protein-bound aminomethyl moiety to form glycine is strongly inhibited Gallus gallus
Fe2+ 0.1 mM, 20% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) Gallus gallus
additional information no significant inhibition: Mn2+, Mg2+ Gallus gallus
Ni2+ 0.1 mM, 84% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) Gallus gallus
Zn2+ 0.1 mM, 99% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein), competitive with both bicarbonate and H-protein and noncompetitive with glycine. Of the two partial reactions, decarboxylation of glycine yielding the H-protein-bound aminomethyl moiety is not significantly affected, but carboxylation of the H-protein-bound aminomethyl moiety to form glycine is strongly inhibited Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
 gel filtration, component P-protein Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus P15505 i.e. component P-protein, glycine dehydrogenase, cf. EC 1.4.4.2
-
Gallus gallus P15505 and P11183 and P28337 P15505 i.e. glycine dehydrogenase component P-protein, cf., EC 1.4.4.2, P11183 i.e. component H-protein, P28337 i.e. aminomethyltransferase component T-protein, cf. EC 2.1.2.10
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

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 2 * 100000, SDS-PAGE, component P-protein Gallus gallus

Synonyms

Synonyms Comment Organism
GCSH
-
 Gallus gallus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate 1 molecule per subunit of component P-protein Gallus gallus

pI Value

Organism Comment pI Value Maximum pI Value
Gallus gallus isoelectric focussing, component P-protein
-
 7.2

General Information

General Information Comment Organism
physiological function the isolated component P-protein can bind glycine and catalyze glycine decarboxylation but at extremely low rate. The product of glycine decarboxylation is methylamine. Methylamine can bind to P-protein, inhibiting the glycine decarboxylation. P-protein alone can also slightly catalyze the exchange of carboxyl carbon of glycine with CO2 and the exchange obeys a pingpong mechanism Gallus gallus