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Literature summary extracted from

  • Hasse, D.; Hagemann, M.; Andersson, I.; Bauwe, H.
    Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803 (2010), Acta Crystallogr. Sect. F, 66, 187-191.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.4.2 expression of the His-tagged enzyme in Escherichia coli Synechocystis sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.4.2 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.4.2 215000
-
-
 Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.4.2 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

EC Number Organism UniProt Comment Textmining
1.4.4.2 Synechocystis sp. P74416
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.4.2 recombinant His-tagged enzyme from Escherichia coli by nickel affinity and ion exchange chromatography, and gel filtration Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.4.2 glycine + H-protein-lipoyllysine
-
 Synechocystis sp. H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
 ?
1.4.4.2 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

EC Number Subunits Comment Organism
1.4.4.2 dimer
-
 Synechocystis sp.

Synonyms

EC Number Synonyms Comment Organism
1.4.4.2 glycine decarboxylase
-
 Synechocystis sp.
1.4.4.2 More glycine decarboxylase, or P-protein, is part of the glycine cleavage system, GCS Synechocystis sp.
1.4.4.2 P-protein
-
 Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.4.2 pyridoxal 5'-phosphate P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor Synechocystis sp.

General Information

EC Number General Information Comment Organism
1.4.4.2 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.
1.4.4.2 additional information glycine decarboxylase, or P-protein, is part of the glycine cleavage system, GCS Synechocystis sp.