首页> 外文期刊>Journal of the American Chemical Society >MgF_3~- and α-Galactose 1-Phosphate in the Active Site of β-Phosphoglucomutase Form a Transition State Analogue of Phosphoryl Transfer
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MgF_3~- and α-Galactose 1-Phosphate in the Active Site of β-Phosphoglucomutase Form a Transition State Analogue of Phosphoryl Transfer

机译:β-磷酸葡萄糖变位酶活性位点中的MgF_3〜-和α-半乳糖1-磷酸形成磷酸转移的过渡态类似物

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摘要

Enzyme catalyzed phosphoryl transfer reactions play integral roles in metabolism, regulation, and cell signaling and are associated with the largest enzymatic rate enhancements yet known. Tri-fluoromagnesate (MgF_3~-) has recently been identified as a trigonal planar mimic for the PO_3~- group in transition states (TS) for several of these enzymes. Its occurrence is likely to be even more widespread since transition state analogue (TSA) structures previously thought to contain AlF_3 most likely instead contain MgF_3~-.
机译:酶催化的磷酸基转移反应在代谢,调节和细胞信号传导中起着不可或缺的作用,并且与已知最大的酶速率提高相关。三氟镁酸酯(MgF_3--)最近被确定为这些酶中的几种在过渡态(TS)下PO_3--基的三角平面模拟物。由于以前被认为包含AlF_3的过渡态类似物(TSA)结构最有可能包含MgF_3〜-,因此它的出现可能更加广泛。

著录项

  • 来源
    《Journal of the American Chemical Society》 |2009年第45期|16334-16335|共2页
  • 作者单位

    Department of Molecular Biology & Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom;

    Department of Molecular Biology & Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom;

    European Synchrotron Radiation Facility, 6 rue Jules Horowitz, F-38043 Grenoble, France;

    Department of Chemistry, University of Sheffield, Sheffield S3 7HF, United Kingdom;

    Department of Molecular Biology & Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom;

    Department of Molecular Biology & Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom Department of Chemistry, Manchester Interdisciplinary Biocentre, University of Manchester, Manchester, Ml 7DN, United Kingdom;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
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  • 入库时间 2022-08-18 03:17:29

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