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

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Hwang H,Kim S,Yoon S,Ryu Y,Lee SY,Kim TD

doi

10.1016/j.ijbiomac.2009.12.010

subject

Has Abstract

pub_date

2010-03-01 00:00:00

pages

145-52

issue

2

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(10)00002-4

journal_volume

46

pub_type

杂志文章

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