Analysis of ping-pong reaction mechanisms by positional isotope exchange. Application to galactose-1-phosphate uridyltransferase.
Open Access
- 1 September 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (25) , 12092-12095
- https://doi.org/10.1016/s0021-9258(18)45320-3
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- The mechanism of the adenylosuccinate synthetase reaction as studied by positional isotope exchange.Journal of Biological Chemistry, 1984
- A positional isotope exchange study of the argininosuccinate lyase reactionBiochemistry, 1984
- Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM—A flexible, portable systemAnalytical Biochemistry, 1983
- 18O and 17O Effects on 31P NMR as Probes of Enzymatic Reactions of Phosphate CompoundsAnnual Review of Biophysics and Bioengineering, 1982
- Phosphorus-31 nuclear magnetic resonance application to positional isotope exchange reactions catalyzed by Escherichia coli carbamoyl-phosphate synthetase: analysis of forward and reverse enzymic reactionsBiochemistry, 1980
- Stereochemical courses of nucleotidyltransferase and phosphotransferase action. Uridine diphosphate glucose pyrophosphorylase, galactose-1-phosphate uridylyltransferase, adenylate kinase, and nucleoside diphosphate kinaseBiochemistry, 1979
- Evidence that carboxyphosphate is a kinetically competent intermediate in the carbamyl phosphate synthetase reaction.Journal of Biological Chemistry, 1979
- A convenient synthesis of crystalline potassium phosphate-18O4 (monobasic) of high isotopic purityJournal of Labelled Compounds and Radiopharmaceuticals, 1978
- A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions. Glutamine synthetase.Journal of Biological Chemistry, 1976
- Galactose-1-phosphate uridylyltransferase. Rate studies confirming a uridylyl-enzyme intermediate on the catalytic pathwayBiochemistry, 1974