In:
FEBS Letters, Wiley, Vol. 368, No. 2 ( 1995-07-17), p. 315-320
Abstract:
In order to investigate the hydrogen‐bonding interactions between Escherichia coli ribonuclease HI and the 2′‐hydroxyl functions of the substrate, oligonucleotide duplexes containing 2′‐amino‐2′‐deoxyuridine or 2′‐fluoro‐2′‐deoxyuridine at a specific site were used, and their affinities for the enzyme were determined by kinetic analyses. The results indicate that the hydroxyl groups of the nucleoside 3′‐adjacent to the cleaved phosphodiester linkage and the second nucleoside 5′ to the cleaved phosphodiester act as both a proton donor and an acceptor and as a proton acceptor, respectively, in the enzyme‐substrate complex. A molecular model was constructed using the interactions derived from the results.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(95)00683-Z
Language:
English
Publisher:
Wiley
Publication Date:
1995
detail.hit.zdb_id:
1460391-3
SSG:
12
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