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Publication Abstract from PubMed

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Here, the full-length GAPDH type 1 from Escherichia coli (EcGAPDH1) was cloned and overexpressed, and the protein was purified. Biochemical analyses found that the optimum reaction temperature and pH of EcGAPDH1 were 55 degrees C and 10.0, respectively. The protein has a certain amount of thermostability. Crystals of EcGAPDH1 were obtained using the sitting-drop vapor-diffusion technique and X-ray diffraction data were collected to 1.88 A resolution. Characterization of the crystals showed that they belonged to space group P41212, with unit-cell parameters a = b = 89.651, c = 341.007 A, alpha = beta = gamma = 90 degrees . The structure of EcGAPDH1 contains four subunits, each of which includes an N-terminal NAD(+)-binding domain and a C-terminal catalytic domain. Analysis of the NAD(+)-bound form showed some differences between the structures of EcGAPDH1 and human GAPDH. As EcGAPDH1 shares 100% identity with GAPDH from Shigella sonnei, its structure may help in finding a drug for the treatment of shigellosis.

Characterization and structure of glyceraldehyde-3-phosphate dehydrogenase type 1 from Escherichia coli.,Zhang L, Liu MR, Yao YC, Bostrom IK, Wang YD, Chen AQ, Li JX, Gu SH, Ji CN Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):406-413. doi:, 10.1107/S2053230X20010067. Epub 2020 Aug 19. PMID:32880588^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.