Phosphodiester Cleavage in Ribonuclease H Occurs via an Associative Two-Metal-Aided Catalytic Mechanism
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چکیده
منابع مشابه
Atomistic details of the phosphodiester cleavage of ribonuclease H
RNase H belongs to the nucleotidyl-transferase (NT) superfamily and in the presence of divalent metal ions, preferably Mg it catalyzes the hydrolysis of phosphodiester linkages of the RNA strand in the DNA:RNA hybrid duplex. RNase H activity is encoded as a part of the reverse transcriptase (RT) that converts a retroviral single strained RNA genome into double strained DNA. Due to the RNase H a...
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The natural substrate cleaved by the hepatitis delta virus (HDV) ribozyme contains a 3',5'-phosphodiester linkage at the cleavage site; however, a 2',5'-linked ribose-phosphate backbone can also be cleaved by both trans-acting and self-cleaving forms of the HDV ribozyme. With substrates containing either linkage, the HDV ribozyme generated 2',3'-cyclic phosphate and 5'-hydroxyl groups suggestin...
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In this study, the hydrolytic reaction mechanism of HPNP by two effective mononuclear Zn(II) catalysts was explored by using density functional calculations. With the assumption that the active catalyst is in Zn-aqua form, the water-assisted proton transfer mode was found to be energetically the most favorable one for both the catalysts among three possible reaction pathways. The rate-limiting ...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2008
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja8005786