Multisubstrate analogs for deoxynucleoside kinases. Triphosphate end products and synthetic bisubstrate analogs exhibit identical modes of binding and are useful probes for distinguishing kinetic mechanisms.
Open Access
- 1 December 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (34) , 15836-15843
- https://doi.org/10.1016/s0021-9258(18)66639-6
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Distinct sites for deoxyguanosine and deoxyadenosine phosphorylation on a monomeric kinase from Lactobacillus acidophilusBiochemistry, 1984
- A new system for washing ion-exchange paper disks used in radiochemical enzyme assaysAnalytical Biochemistry, 1984
- Arginyl residues and anion binding sites in proteinsMolecular and Cellular Biochemistry, 1979
- [18] Use of competitive inhibitors to study substrate binding orderPublished by Elsevier ,1979
- Binding of reactive intermediate analogs to enzymesJournal of Theoretical Biology, 1978
- [44] Deoxynucleoside kinases from Lactobacillus acidophilus R-26Published by Elsevier ,1978
- Inhibition of hexokinase by multisubstrate analogsBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Non-allosteric regulation of the uridine kinase from seeds of Zea maysBiochimica et Biophysica Acta (BBA) - Enzymology, 1975
- Inhibition of rabbit skeletal muscle adenylate kinase by the transition state analogue, P1,P4-di(adenosine-5′)tetraphosphateBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- Analog approaches to the structure of the transition state in enzyme reactionsAccounts of Chemical Research, 1972