کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1357207 | 981212 | 2005 | 6 صفحه PDF | دانلود رایگان |

Histone deacetylases (HDACs) have recently attracted considerable interest as targets in the treatment of cell proliferative diseases such as cancer. In the present work, the chemical properties of the active site of HDAC were theoretically investigated at a high computational level. Evidence was gathered for a novel catalytic mechanism, which differs from a previous proposal in the native protonation state of the His–Asp dyads, and in the deprotonation of water as a distinct step in the mechanism.
Computational study of the active site of HDAC at a high level of theory, yielding evidence for a novel catalytic mechanism that differs from a previous proposal in the native protonation state of the enzyme, and in the deprotonation of water as a distinct step in the mechanism.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry - Volume 13, Issue 12, 2 June 2005, Pages 3987–3992