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The enantioselectivities of the active and allosteric sites of mammalian ribonucleotide reductase.

Authors :
He J
Roy B
Périgaud C
Kashlan OB
Cooperman BS
Source :
The FEBS journal [FEBS J] 2005 Mar; Vol. 272 (5), pp. 1236-42.
Publication Year :
2005

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 and L-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 corresponding D-enantiomers. These results demonstrate the potential of L-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 for L-ADP and no inhibitory activity for N3-L-dUDP, demonstrating the greater stereochemical stringency at the active site with respect to catalytic activity.

Details

Language :
English
ISSN :
1742-464X
Volume :
272
Issue :
5
Database :
MEDLINE
Journal :
The FEBS journal
Publication Type :
Academic Journal
Accession number :
15720397
Full Text :
https://doi.org/10.1111/j.1742-4658.2005.04557.x