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学科主题: 生命有机化学
题名: Detailed active site configuration of a new crystal form of methanol dehydrogenase from methylophilus W3A1 at 1.9 A resolution
其他题名: 从 Methylophilus W3A1 提取的甲醇脱氢酶新晶型的1.9A分辨率的活性中心精细构型
作者: Xia ZX(夏宗芗) ; He YN(何勇宁) ; Dai WW(戴伟文) ; Scott A. Wthite ; Geoffrey D. Boyd ; F. Scott Mathews
通讯作者: F. Scott Mathews
刊名: Biochemistry
发表日期: 1999-01-01
卷: 38, 期:4, 页:1214-1220
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所生命有机国家开放实验室; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110
英文摘要: The three-dimensional structure of a new crystal form of methanol dehydrogenase from methylophilus W3A1 has been obtained in the presence of substrate using data recorded at a synchrotron. The structure of this ~140 Kda heterotetramer, refined at 1.9A resolution, revelas the detailed configuration of its redox cofactor, pyrroloquinoline quinone (PQQ). C4, one of the oxygen-bearing atoms of this orthoquinone is in a planar configuration while C5, which bears the other quinone oxygen, is tetrahedral, suggesting thar the PQQ is in the semiquinone redox state. The substrate binding site has been identified close to PQQ and to the side chain of Asp297, the putative active site base. The proximity of the hydroxyl of methanol to C5 of PQQ compared to the greater seqaration of the substrate methyl group from C5 supports the addition-elimination reaction mechanism involving a hemiketal intermediate.
语种: 英语
相关网址: 查看原文
内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/23654
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
Xia ZX,He YN,Dai WW,et al. Detailed active site configuration of a new crystal form of methanol dehydrogenase from methylophilus W3A1 at 1.9 A resolution[J]. Biochemistry,1999,38(4):1214-1220.
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