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Cloning and Characterization of Fructose-1,6-Bisphosphate Aldolase from Euphausia superba

文献类型： 外文期刊

作者： Xia, Jikun 1 ; Xin, Wanmeng 3 ; Wang, Fang 2 ; Xie, Wancui 1 ; Liu, Yi 3 ; Xu, Jiakun 2 ;

作者机构： 1.Qingdao Univ Sci & Technol, Coll Marine Sci & Biol Engn, Qingdao 266042, Peoples R China

2.Chinese Acad Fishery Sci, Key Lab Sustainable Dev Polar Fisheries, Yellow Sea Fisheries Res Inst,Minist Agr & Rural, Lab Marine Drugs & Byprod,Pilot Natl Lab Marine S, Qingdao 266071, Peoples R China

3.Hubei Univ, Sch Life Sci, State Key Lab Biocatalysts & Enzyme Engn, Wuhan 430062, Peoples R China

关键词： fructose-1; 6-bisphosphate aldolase; Euphausia superba; heterologous expression; molecular simulation; point mutation

期刊名称：INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES （ 影响因子：6.208； 五年影响因子：6.628 ）

ISSN：

年卷期： 2022 年 23 卷 18 期

页码：

收录情况： SCI

摘要： Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) is a highly conserved enzyme that is involved in glycolysis and gluconeogenesis. In this study, we cloned the fructose-1,6-bisphosphate aldolase gene from Euphausia superba (EsFBA). The full-length cDNA sequence of EsFBA is 1098 bp long and encodes a 365-amino-acid protein. The fructose-1,6-bisphosphate aldolase gene was expressed in Escherichia coli (E. coli). A highly purified protein was obtained using HisTrap HP affinity chromatography and size-exclusion chromatography. The predicted three-dimensional structure of EsFBA showed a 65.66% homology with human aldolase, whereas it had the highest homology (84.38%) with the FBA of Penaeus vannamei. Recombinant EsFBA had the highest activity at 45 degrees C and pH 7.0 in phosphate buffer. By examining the activity of metal ions and EDTA, we found that the effect of metal ions and EDTA on EsFBA's enzyme activity was not significant, while the presence of borohydride severely reduced the enzymatic activity; thus, EsFBA was confirmed to be a class I aldolase. Furthermore, targeted mutations at positions 34, 147, 188, and 230 confirmed that they are key amino acid residues for EsFBA.

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