Department of Chemistry, State University of Ponta Grossa, Ponta Grossa - PR, 84030-900, Brazil.
Department of Education, Federal Technological University of Paraná, Ponta Grossa - PR, 84016-210, Brazil.
Biochimie. 2021 May;184:18-25. doi: 10.1016/j.biochi.2021.01.014. Epub 2021 Jan 30.
The enzyme Glyceraldehyde-3-Phosphate Dehydrogenase from Schistosoma mansoni (SmGAPDH) is characterized as a therapeutical target for schistosomiasis. In this context, we report here the experimental structure, structural analyses and comparisons of SmGAPDH, the first one from a Platyhelminth. The enzyme was expressed, purified and assayed for crystallization, what allowed the obtainment of crystals of sufficient quality to collect X-ray diffraction data up to 2.51 Å resolution. SmGAPDH is the only GAPDH to present the sequence NNR (its residues 114-116) which leads to (especially R116) a hydrogen bond network that possibly reflects on the flexibility of residues to interact with the adenine part of NAD, speculated to be important for differential drug design.
曼氏血吸虫甘油醛-3-磷酸脱氢酶（SmGAPDH）是一种有治疗潜力的血吸虫病治疗靶点。在此，我们报告了第一个来自扁形动物的 SmGAPDH 的实验结构、结构分析和比较。该酶经表达、纯化并进行结晶分析，获得了具有足够质量的晶体，可收集高达 2.51 Å分辨率的 X 射线衍射数据。SmGAPDH 是唯一具有 NNR 序列（其残基 114-116）的 GAPDH，这导致（特别是 R116）形成氢键网络，可能反映了残基与 NAD 的腺嘌呤部分相互作用的灵活性，这被推测对药物设计的差异很重要。
