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The enantioselectivities of the active and allosteric sites of mammalian ribonucleotide reductase.
- 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.
- Subjects :
- Adenosine Diphosphate chemistry
Adenosine Diphosphate metabolism
Adenosine Triphosphate chemistry
Allosteric Site
Animals
Binding Sites
Cytidine Diphosphate chemistry
Cytidine Diphosphate metabolism
Mice
Protein Binding
Protein Subunits metabolism
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Ribonucleoside Diphosphate Reductase metabolism
Substrate Specificity genetics
Adenosine Triphosphate metabolism
Allosteric Regulation
Protein Subunits chemistry
Ribonucleoside Diphosphate Reductase chemistry
Subjects
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