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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2021.12
- 수록면
- 67 - 71 (5page)
- DOI
- 10.34184/kssb.2021.9.4.67
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초록· 키워드
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S -formylglutathione hydrolase (SFGH) is an esterase that hydrolyzes S -formylglutathione into formic acid and glutathione. As SFGHs are also able to hydrolyze thioesters as well as non-thioester substrates, they have attracted considerable attention as potential biocatalysts. Although the substrate specificity of various SFGHs has been determined, the detailed structural differences relating to substrate preference remain unclear. Here, we present overexpression, purification, and preliminary X-ray crystallographic data for an SFGH from Variovorax sp. PAMC 28711 (VaSFGH). The VaSFGH protein was over-expressed in Escherichia coli and successfully crystallized in 0.2 M sodium chloride, 0.1 M Bis-Tris:HCl (pH 6.5), and 20% (w/v) PEG 3350. A complete native X-ray diffraction dataset was collected up to 2.38 A resolution and processed in the C2 space group with unit-cell parameters a = 53.2 A, b = 76.4 A, c = 199.9 A, α = 90°, β = 90.2°, and γ = 90°. Moreover, VaSFGH exhibited higher esterase activity toward shorter-chain esters. Based on its structural determination, future studies will elucidate the substrate-binding mechanism and specificity of VaSFGH at the molecular level.
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참고문헌 (20)
참고문헌 신청
Adams, P. D. / 2010 / PHENIX : a comprehensive Python-based system for macromolecular structure solution / Acta Crystallogr D Biol Crystallogr 66:213~221
Chen, N. H. / 2013 / A glutathione-dependent detoxification system is required for formaldehyde resistance and optimal survival of Neisseria meningitidis in biofilms / Antioxid Redox Signal 18:743~755
Cummins, I. / 2006 / Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase / J Mol Biol 359:422~432
Emsley, P. / 2004 / Coot : model-building tools for molecular graphics / Acta Crystallogr D Biol Crystallogr 60:2126~2132
Gonzalez, C. F. / 2006 / Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG / J Biol Chem 281:14514~14522
Chen, N. H. / 2013 / A glutathione-dependent detoxification system is required for formaldehyde resistance and optimal survival of Neisseria meningitidis in biofilms / Antioxid Redox Signal 18:743~755
Cummins, I. / 2006 / Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase / J Mol Biol 359:422~432
Emsley, P. / 2004 / Coot : model-building tools for molecular graphics / Acta Crystallogr D Biol Crystallogr 60:2126~2132
Gonzalez, C. F. / 2006 / Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG / J Biol Chem 281:14514~14522
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