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characterizing the Fused TvG6PD::6PGL protein from the protozoan, and effects of the NADP molecule on enzyme stability.

Characterizing the Fused TvG6PD::6PGL Protein from the Protozoan , and Effects of the NADP Molecule on Enzyme Stability.

机构信息

Laboratorio de Bioquímica Genética, Instituto Nacional de Pediatría, Secretaría de Salud, 04530 Ciudad de México, Mexico.

Posgrado en Ciencias Biológicas, Universidad Nacional Autónoma de México, 04510 Ciudad de México, Mexico.

出版信息

Int J Mol Sci. 2020 Jul 8;21(14):4831. doi: 10.3390/ijms21144831.

DOI:10.3390/ijms21144831
PMID:32650494
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7402283/
Abstract

This report describes a functional and structural analysis of fused glucose-6-phosphate dehydrogenase dehydrogenase-phosphogluconolactonase protein from the protozoan (). The glucose-6-phosphate dehydrogenase () gene from . was isolated by PCR and the sequence of the product showed that is fused with gene. The fused Tv:: gene was cloned and overexpressed in a heterologous system. The recombinant protein was purified by affinity chromatography, and the oligomeric state of the TvG6PD::6PGL protein was found as tetramer, with an optimal pH of 8.0. The kinetic parameters for the G6PD domain were determined using glucose-6-phosphate (G6P) and nicotinamide adenine dinucleotide phosphate (NADP) as substrates. Biochemical assays as the effects of temperature, susceptibility to trypsin digestion, and analysis of hydrochloride of guanidine on protein stability in the presence or absence of NADP were performed. These results revealed that the protein becomes more stable in the presence of the NADP. In addition, we determined the dissociation constant for the binding () of NADP in the protein and suggests the possible structural site in the fused TvG6PD::6PGL protein. Finally, computational modeling studies were performed to obtain an approximation of the structure of TvG6PD::6PGL. The generated model showed differences with the GlG6PD::6PGL protein (even more so with human G6PD) despite both being fused.

摘要

本报告描述了原生动物 （）中融合葡萄糖-6-磷酸脱氢酶脱氢酶-磷酸葡萄糖酸内酯酶蛋白的功能和结构分析。通过 PCR 从. 中分离出葡萄糖-6-磷酸脱氢酶（）基因，产物的序列表明它与 基因融合。克隆并在异源系统中过表达融合的 Tv:: 基因。通过亲和层析纯化重组蛋白，发现 TvG6PD::6PGL 蛋白的寡聚状态为四聚体，最适 pH 值为 8.0。使用葡萄糖-6-磷酸（G6P）和烟酰胺腺嘌呤二核苷酸磷酸（NADP）作为底物测定 G6PD 结构域的动力学参数。进行了生化测定，如温度、对胰蛋白酶消化的敏感性以及盐酸胍对 NADP 存在或不存在时蛋白质稳定性的分析。这些结果表明，在 NADP 的存在下，蛋白质变得更加稳定。此外，我们确定了蛋白中 NADP 结合（）的解离常数，并提出了融合的 TvG6PD::6PGL 蛋白中可能的结构位点。最后，进行了计算建模研究以获得 TvG6PD::6PGL 的结构近似值。生成的模型显示与 GlG6PD::6PGL 蛋白存在差异（与人类 G6PD 差异更大），尽管它们都融合了。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9848/7402283/f284046f44c3/ijms-21-04831-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9848/7402283/45fa0f75f6ee/ijms-21-04831-g001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9848/7402283/97ba7d9b2d87/ijms-21-04831-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9848/7402283/e5f803667485/ijms-21-04831-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9848/7402283/76d936439f17/ijms-21-04831-g004.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9848/7402283/f284046f44c3/ijms-21-04831-g009.jpg

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