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- Title
The enantioselectivities of the active and allosteric sites of mammalian ribonucleotide reductase.
- Authors
He, Jian; Roy, Béatrice; Périgaud, Christian; Kashlan, Ossama B.; Cooperman, Barry S.
- Abstract
Here we examine the enantioselectivity of the allosteric and substrate binding sites of murine ribonucleotide reductase (mRR).l-ADP binds to the active site andl-ATP binds to both the s- and a-allosteric sites of mR1 with affinities that are only three- to 10-fold weaker than the values for the correspondingd-enantiomers. These results demonstrate the potential ofl-nucleotides for interacting with and modulating the activity of mRR, a cancer chemotherapeutic and antiviral target. On the other hand, we detect no substrate activity forl-ADP and no inhibitory activity for N3-l-dUDP, demonstrating the greater stereochemical stringency at the active site with respect to catalytic activity.
- Subjects
ENANTIOSELECTIVE catalysis; ALLOSTERIC proteins; DEOXYRIBONUCLEOTIDES; BINDING sites; NUCLEOTIDES; STEREOCHEMISTRY
- Publication
FEBS Journal, 2005, Vol 272, Issue 5, p1236
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04557.x