Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Nuclease S1 hydrolyzes the Sp-diastereomer of 5'-O-(2'-deoxyadenosyl)-3'-O-thymidyl phosphorothioate in H2(18)O to [18O]deoxyadenosine 5'-O-phosphorothioate which can be phosphorylated enzymatically to the Sp-diastereomer of [alpha-18O]deoxyadenosine 5'-O-(1-thiotriphosphate). 31P nmr spectroscopy shows the oxygen-18 in this compound to be in a nonbridging position at the alpha-phosphorus, indicating that the hydrolysis reaction catalyzed by nuclease S1 proceeds with inversion of configuration at phosphorus. This result is compatible with a direct nucleophilic attack of H2O at phosphorus without the involvement of a covalent enzyme intermediate.

Original publication

DOI

10.1016/s0021-9258(18)33051-5

Type

Journal article

Journal

The Journal of biological chemistry

Publication Date

02/1983

Volume

258

Pages

1758 - 1760

Keywords

Aspergillus oryzae, Oxygen Isotopes, Endonucleases, Oligonucleotides, Oligodeoxyribonucleotides, Chromatography, High Pressure Liquid, Substrate Specificity, Kinetics, Single-Strand Specific DNA and RNA Endonucleases