Diphosphopyridine nucleotide: a cofactor for the polynucleotide-joining enzyme from Escherichia coli.
- 1 June 1967
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 57 (6), 1700-1704
- https://doi.org/10.1073/pnas.57.6.1700
Abstract
The DPN is a cofactor for the polynucleotide-joining enzyme from E. coli. The apparent Km (1 x 10-7 [image]) is of the same order of magnitude as the Km for the polydeoxythymidylate substrate (2.5 x 10-8 [image]); DPNH and the thionicotinamide derivative of DPN while active had Km values 7-fold greater than DPN. The other analogues of DPN including TPN were inactive.This publication has 4 references indexed in Scilit:
- Linkage of polynucleotides through phosphodiester bonds by an enzyme from Escherichia coli.Proceedings of the National Academy of Sciences, 1967
- Chemical Properties of 3-Substituted Pyridine Analogues of Diphosphopyridine NucleotideJournal of Biological Chemistry, 1959
- STUDIES ON POLYNUCLEOTIDES .3. ENZYMIC DEGRADATION - SUBSTRATE SPECIFICITY AND PROPERTIES OF SNAKE VENOM PHOSPHODIESTERASE1959
- NEUROSPORA DIPHOSPHOPYRIDINE NUCLEOTIDASEJournal of Biological Chemistry, 1951