Biochemistry. by Dunitz J.D.

By Dunitz J.D.

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Ribonucleoside Triphosphate Reductase ]rom Pithomyces chartarum The reductase detected in crude extracts of this fungus showed barely detectable activity with pufine nucleoside diphosphates and was most active with ATP and GTP (71). B. Ribonucleoside Diphosphate Reductases Adenosylcobalamin-dependent reductases which utilize ribonucleoside diphosphates as substrates have been detected in three different microorganisms : Rhizobium meliloti (82), Bacillus megaterium (10) and Corynebacterium nephridii (83).

Leichmannii is subject to allosteric control by the deoxyribonucleotide products. In the absence of effectors the enzyme reduces the nucleotide substrates at markedly different rates; however these rates are selectively modified by deoxyribonucleotide triphosphates which function as specific activators. Stimulation of ATP reduction is caused by dGTP, of CTP by dATP and of UTP by dCTP (52, 74). The reduction of GTP, the best substrate, is not affected significantly by any of the common deoxyribonucleotides.

J. Biol. Chem. 247, 3336 (1972). 3. El]ord, H. , Morris, H. P. : J. Biol. Chem. 245, 5228 (1970). 4. El/ord, H. : Advan. Enzyme Regulation 70, 19 (1972). 5. Reichard, P. : European J. Biochem. 3, 259 (1968). 6. Blahley, R. : J. Biol. Chem. 240, 2173 (1965). 7. Gleason, F. , Hogenhamp, H. P. C. : Biochim. Biophys. Acta 277, 466 (1972). 8. Abeles, R. , Beck, W. : J. Biol. Chem. 2d2, 3589 (1967). 9. Cowles, J. , Evans, H.

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