KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
40 | - |
glycine | - |
Gallus gallus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Gallus gallus | 5739 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
100000 | - |
alpha2, 2 * 100000, SDS-PAGE | Gallus gallus |
208000 | - |
sucrose density gradient centrifugation | Gallus gallus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + lipoylprotein | Gallus gallus | reaction is stimulated by lipoic acid which is a functional group of the H-protein | S-aminomethyldihydrolipoylprotein + CO2 | - |
? | |
glycine + lipoylprotein | Gallus gallus | glycine decarboxylation catalyzed by P-protein alone is extremely low | S-aminomethyldihydrolipoylprotein + CO2 | - |
? | |
glycine + lipoylprotein | Gallus gallus | lipoyl protein: H-protein, lipoamide can also act as acceptor | S-aminomethyldihydrolipoylprotein + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Gallus gallus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2 | H-protein ping-pong mechanism | Gallus gallus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Gallus gallus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
4.13 | - |
- |
Gallus gallus |
Storage Stability | Organism |
---|---|
-20°C, several weeks | Gallus gallus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + lipoylprotein | reaction is stimulated by lipoic acid which is a functional group of the H-protein | Gallus gallus | S-aminomethyldihydrolipoylprotein + CO2 | - |
? | |
glycine + lipoylprotein | glycine decarboxylation catalyzed by P-protein alone is extremely low | Gallus gallus | S-aminomethyldihydrolipoylprotein + CO2 | - |
? | |
glycine + lipoylprotein | lipoyl protein: H-protein, lipoamide can also act as acceptor | Gallus gallus | S-aminomethyldihydrolipoylprotein + CO2 | - |
? | |
additional information | P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein | Gallus gallus | ? | - |
? | |
additional information | the glycine cleavage system consists of 4 protein components: 1. P-protein is a pyridoxal containing protein: a Schiff base is formed between the hydroxyl group of the pyridoxal phosphate and the alpha-NH2 of glycine, the amino group and the alpha-carbon of the glycine are transferred to the lipoamide cofactor of the second enzyme of the complex the H-protein, the alpha-carbonyl group of glycine is lost as CO2, 2. H-protein, 3. T-protein: catalyzes the passage of alpha-carbon from lipoamide of H protein to tetrahydrofolate, alpha-NH2 from glycine is lost as NH4+, 4. L-protein: catalyzes oxidation of reduced lipoamide back to its original form with concomitant reduction of NAD+ to NADH | Gallus gallus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | alpha2, 2 * 100000, SDS-PAGE | Gallus gallus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Gallus gallus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | bound | Gallus gallus |