| Literature DB >> 20060410 |
Heejin Hwang1, Seungbum Kim, Sangyoung Yoon, Yeonwoo Ryu, Sang Yoon Lee, T Doohun Kim.
Abstract
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 (Ser(10), Asp(187), and His(190)) and oxyanion holes (Ser(10)-Gly(50)-Asn(90)). The wild type enzyme was able to hydrolyze p-nitrophenyl acetate, alpha- and beta-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. 2010 Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID： 20060410 DOI： 10.1016/j.ijbiomac.2009.12.010
Source DB: PubMed Journal: Int J Biol Macromol ISSN： 0141-8130 Impact factor: 6.953