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

Authors
Hwang, H; Kim, S; Yoon, S; Ryu, Y; Lee, SY; Kim, TD
Citation
International journal of biological macromolecules, 46(2):145-152, 2010
Journal Title
International journal of biological macromolecules
ISSN
0141-81301879-0003
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.
MeSH terms
Amino Acid SequenceCarboxylic Ester Hydrolases/*chemistry/*metabolism/ultrastructureCircular DichroismElectrophoresis, Polyacrylamide GelEnzyme AssaysLightMolecular Sequence DataProtein ConformationScattering, RadiationSequence AlignmentSequence Analysis, ProteinSinorhizobium meliloti/*enzymologySolventsSpectrometry, FluorescenceStaining and LabelingStereoisomerismSubstrate Specificity
DOI
10.1016/j.ijbiomac.2009.12.010
PMID
20060410
Appears in Collections:
Journal Papers > Research Organization > Chronic Inflammatory Disease Research Center
AJOU Authors
이, 상윤
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