Cloned (Comment) | Organism |
---|---|
expression of the His-tagged enzyme in Escherichia coli | Synechocystis sp. |
Crystallization (Comment) | Organism |
---|---|
purified recombinant His-tagged enzyme, hanging drop vapour diffusion, 18°C, 0.004 ml of 40/mg/ml protein in 20 mM Tris-HCl, pH 7.8, 50 mM sodium chloride, and 10 mM 2-mercaptoethanol, are mixed with 0.004 ml of reservoir solution containing 100 mM Tris-HCl pH 7.75, 15-25% PEG 3350, 0.15-0.3 M CsCl or LiCl and 10 mM 2-mercaptoethanol, equilibration over 1 ml reservoir solution, method optimization, 1-3 days, streak-seeding at 20°C, X-ray diffraction structure determination and analysis at 2.1 A resolution | Synechocystis sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
215000 | - |
- |
Synechocystis sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + H-protein-lipoyllysine | Synechocystis sp. | P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor. CO2 is released in the reaction and the residual aminomethyl group is bound to the oxidized lipoamide arm of H-protein | H-protein-S-aminomethyldihydrolipoyllysine + CO2 | the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | P74416 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli by nickel affinity and ion exchange chromatography, and gel filtration | Synechocystis sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + H-protein-lipoyllysine | - |
Synechocystis sp. | H-protein-S-aminomethyldihydrolipoyllysine + CO2 | - |
? | |
glycine + H-protein-lipoyllysine | P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor. CO2 is released in the reaction and the residual aminomethyl group is bound to the oxidized lipoamide arm of H-protein | Synechocystis sp. | H-protein-S-aminomethyldihydrolipoyllysine + CO2 | the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism | ? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Synechocystis sp. |
Synonyms | Comment | Organism |
---|---|---|
glycine decarboxylase | - |
Synechocystis sp. |
More | glycine decarboxylase, or P-protein, is part of the glycine cleavage system, GCS | Synechocystis sp. |
P-protein | - |
Synechocystis sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor | Synechocystis sp. |
General Information | Comment | Organism |
---|---|---|
metabolism | glycine decarboxylase is a major enzyme that is involved in the C1 metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. GCS is also essential in the plant photorespiratory C2 cycle, which salvages 2-phosphoglycolate resulting from the oxygenation reaction catalysed by ribulose-1,5-bisphosphate carboxylase/oxygenase under atmospheric conditions. The complete GCS reaction cycle requires the cooperation of three different enzymes, P-protein, T-protein and L-protein, and the small heat-stable H-protein, pathway overview | Synechocystis sp. |
additional information | glycine decarboxylase, or P-protein, is part of the glycine cleavage system, GCS | Synechocystis sp. |