Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021

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• 作者：Heejin Hwang ; SeungBum Kim ; Sangyoung Yoon ; Yeonwoo Ryu ; Sang Yoon Lee ; T. Doohun Kim
• 关键词：SGNH-arylesterase ; p-Nitrophenyl acetate ; Structural analysis
• 刊名：International Journal of Biological Macromolecules
• 出版年：2010
• 出版时间：1 March 2010
• 年：2010
• 卷：46
• 期：2
• 页码：145-152
• 全文大小：1309 K

文摘

A novel oligomeric SGNH-arylesterase (Sm23) from Sinorhizobium meliloti 1021 was characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of catalytic triad (Ser¹⁰, Asp¹⁸⁷, and His¹⁹⁰) and oxyanion holes (Ser¹⁰-Gly⁵⁰-Asn⁹⁰). The wild type enzyme was able to hydrolyze p-nitrophenyl acetate, α- and β-naphthyl acetate, while S10A mutant completely lost its activity. Structural properties of Sm23 were investigated using circular dichroism (CD), fluorescence, dynamic light scattering (DLS), chemical cross-linking, electron microscopy (EM), and time of flight (TOF) mass spectrometry. Furthermore, spherical or globular aggregates were observed with 1-butyl-3-methylimidazolium tetrafluoroborate, while amorphous aggregates were formed with 1-butyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide.