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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2017.12
- 수록면
- 132 - 135 (4page)
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초록· 키워드
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Alcohol dehydrogenase (ADH) is one of essential enzymes for all living organisms, and conserved from archaea to mammals.
The most abundant type of ADH is zinc-containing one. All the zinc containing ADHs possess the catalytic zinc site, whilesome have the second, structural zinc site. ADHs require either NAD(H) or NADP(H) as a cofactor. Despite lots of effortsto determine the key residues for cofactor specificity of ADHs, there is no general rule for cofactor specificity so far. Toestablish the general rules for the cofactor specificity of ADHs by structural analysis, we cloned and overexpressed the zincdependent alcohol dehydrogenase from Streptococcus pneumoniae strain D39 (SpADH2) in Escherichia coli. Rod-shapecrystals of SpADH2 were obtained by hanging-drop vapour diffusion from a reservoir solution containing 50 mM Tris-HCl pH8.0, 50 mM NaCl, PEG 3350 15% (w/v) and diffracted to 2.19 A resolution. Crystal belonged to orthorhombic space groupP212121 with unit cell parameters a = 88.2 A, b = 123.2 A, c = 130.4 A and contained four molecules in the asymmetric unit.
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참고문헌 (14)
참고문헌 신청
Adams, P. D / 2010 / PHENIX : a comprehensive Python-based system for macromolecular structure solution / Acta Crystallogr D Biol Crystallogr 66:213~221
Banta, S / 2002 / Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2, 5-diketo-D-gluconic acid reductase A / Protein Eng 15:131~140
Banta, S / 2002 / Optimizing an artificial metabolic pathway : engineering the cofactor specificity of Corynebacterium 2, 5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis / Biochemistry 41:6226~6236
Goihberg, E / 2008 / Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution / Proteins 72:711~719
Hayashi, J / 2015 / Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases / Sci Rep 5:11674
Banta, S / 2002 / Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2, 5-diketo-D-gluconic acid reductase A / Protein Eng 15:131~140
Banta, S / 2002 / Optimizing an artificial metabolic pathway : engineering the cofactor specificity of Corynebacterium 2, 5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis / Biochemistry 41:6226~6236
Goihberg, E / 2008 / Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution / Proteins 72:711~719
Hayashi, J / 2015 / Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases / Sci Rep 5:11674
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