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Structural and Functianal Characterizations of SGNH-family Esterases from Sinorhizobium meliloti
- Author(s)
- 황희진
- Advisor
- 김두헌
- Department
- 일반대학원 분자과학기술학과
- Publisher
- The Graduate School, Ajou University
- Publication Year
- 2010-02
- Language
- eng
- Keyword
- SGNH-superfamily; esterase; GDSL; p-nitrophenyl acetate
- Alternative Abstract
- Novel oligomeric SGNH-arylesterases from Sinorhizobium mellioti, SM23, SM24A and SM24B, were characterized using biochemical and biophysical methods. A sequence comparison of Sm23 with other SGNH members confirmed the presence of the catalytic triad (Ser10, Asp187, and His190) and oxyanion holes (Ser10-Gly50-Asn90). SM24A has a catalytic triad (Ser13, Asp187, and His190), but it does not have a consensus blockⅡ. SM24B as well as Sm23 have four conserved sequence blocks containing the catalytic triad (Ser15, Asp192, and His195), and oxyanion hole residues (Ser15-Gly57-Asn97). All these Enzymes were able to hydrolyze p-nitrophenyl acetate, α-, and β-naphthyl acetate, while the S10A of Sm23 mutant completely losts its activity. Structural properties of Sm23 were investigated using circular dichroism (CD), fluoroscence, dynamic light scattering (DLS), chemical cross-linking, electron microscopy (EM), and time of flight (TOF) mass spectrometry. 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.
- Fulltext
- Appears in Collections:
- Graduate School of Ajou University > Department of Molecular Science and Technology > 3. Theses(Master)
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