Glucose 6-phosphate dehydrogenase

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	**[[1e77]] – LmG6PD (mutant) + G6P<br />		**[[1e77]] – LmG6PD (mutant) + G6P<br />
	**[[1e7y]] – LmG6PD (mutant) + G6P + NADP<br />		**[[1e7y]] – LmG6PD (mutant) + G6P + NADP<br />
-	**[[1qki]], [[2bh9]] – hG6PD + NADP - human<br />	+	**[[1qki]], [[2bh9]], [[5vfl]] – hG6PD + NADP - human<br />
		+	**[[5vg5]] – hG6PD (mutant) + NADP <br />
	**[[2bhl]], [[5ukw]] – hG6PD (mutant) + G6P<br />		**[[2bhl]], [[5ukw]] – hG6PD (mutant) + G6P<br />
	**[[6d24]] – TcG6PD + G6P<br />		**[[6d24]] – TcG6PD + G6P<br />

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Revision as of 09:32, 30 May 2018

spinqualitylabelsall models Structure of glucose 6-phosphate dehydrogenase complex with glucose 6-phosphate and Ca+2 ion (green) (PDB code 1e77). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Glucose 6-phosphate dehydrogenase (G6PD) catalyzes the conversion of glucose 6-phosphate (G6P)to 6-phospho-glucono-1,5-lactone. G6PD uses NAPD as cofactor[1]. G6PD is found in the cytoplasm and its function is protection against oxidative damage caused by metabolism. G6PD is part of the pentose phosphate cycle which is part of the cellular carbohydrate synthesis. See also G6PD (Hebrew). Disease G6PD deficiency is genetically recessive and predisposes toward hemolytic anemia[2]. This disease is not fatal if the carrier maintains a suitable diet and uses appropriate drugs like corticsteroids. G6PD deficiency in red blood cells causes lack of NADPH which results in oxidative damage of the cell membrane and its rupture. Structural highlights (PDB code 1e77), water molecules shown as red spheres. [3]

3D structures of glucose 6-phosphate dehydrogenase

Updated on 30-May-2018

References

1. ↑ Tian WN, Braunstein LD, Pang J, Stuhlmeier KM, Xi QC, Tian X, Stanton RC. Importance of glucose-6-phosphate dehydrogenase activity for cell growth. J Biol Chem. 1998 Apr 24;273(17):10609-17. PMID:9553122
2. ↑ Cappellini MD, Fiorelli G. Glucose-6-phosphate dehydrogenase deficiency. Lancet. 2008 Jan 5;371(9606):64-74. doi: 10.1016/S0140-6736(08)60073-2. PMID:18177777 doi:http://dx.doi.org/10.1016/S0140-6736(08)60073-2
3. ↑ Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR. An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme. Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:11106478