glycine dehydrogenase (aminomethyl-transferring)

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Word Map on EC


[glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine


decarboxylase, glycine, GDC, GDCP, GLDC, GLDH, GLDP, Gly decarboxylase complex, Gly decarboxylase H1, glycine cleavage enzyme complex, glycine cleavage H protein, glycine cleavage system H protein 1, Glycine cleavage system P-protein, glycine decarboxylase, glycine decarboxylase (P-protein), glycine decarboxylase complex, glycine decarboxylase complex H, glycine decarboxylase P-protein, glycine dehydrogenase, glycine dehydrogenase (decarboxylating), glycine-cleavage complex, H protein, H-protein, H1 protein, H2 protein, L protein, More, P protein, P-protein, P-protein (glycine decarboxylase), P-subunit, Protein P1, T protein


     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.4 With a disulfide as acceptor
       glycine dehydrogenase (aminomethyl-transferring)


Crystallization on EC - glycine dehydrogenase (aminomethyl-transferring)

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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
hanging-drop vapour-difffusion method, crystals belong to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 89.5, c = 371.0 A
vapour diffusion method with 30% w/v polyethylene glycol 3350 and 100 mM KSCN as the precipitant. Crystal structure of three forms of P-protein: the apoenzyme at 2.4 A resolution, the holoenzyme at 2.1 A resolution and the holoenzyme in complex with a substrate analog inhibitor (aminooxy)acetate