Literature summary 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 .
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.4.1.27 |
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]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.4.1.27 |
40 |
- |
glycine |
value for the isolated P-protein, pH 6.6, 37°C |
Gallus gallus |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.4.1.27 |
mitochondrion |
- |
Gallus gallus |
5739 |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.4.1.27 |
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 |
|
1.4.1.27 |
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 |
|
1.4.1.27 |
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 |
|
1.4.1.27 |
additional information |
no significant inhibition: Mn2+, Mg2+ |
Gallus gallus |
|
1.4.1.27 |
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 |
|
1.4.1.27 |
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]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.4.1.27 |
200000 |
- |
gel filtration, component P-protein |
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 |
- |
1.4.1.27 |
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
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 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.4.1.27 |
multimer |
2 * 100000, SDS-PAGE, component P-protein |
Gallus gallus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.4.1.27 |
GCSH |
- |
Gallus gallus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.4.1.27 |
pyridoxal 5'-phosphate |
1 molecule per subunit of component P-protein |
Gallus gallus |
|
pI Value
EC Number |
Organism |
Comment |
pI Value Maximum |
pI Value |
---|
1.4.1.27 |
Gallus gallus |
isoelectric focussing, component P-protein |
- |
7.2 |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.4.1.27 |
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 |