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Literature summary for 1.4.4.2 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)

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

Crystallization (Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Synechocystis sp. P74416
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits Comment Organism
dimer
-
Synechocystis sp.

Synonyms

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

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

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.