The binding of N-(phosphonacetyl)-L-aspartate to aspartate carbamoyltransferase of Escherchia Coli
- 31 March 1986
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 136 (2) , 822-826
- https://doi.org/10.1016/0006-291x(86)90514-0
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.Proceedings of the National Academy of Sciences, 1985
- Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.Proceedings of the National Academy of Sciences, 1984
- Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coliJournal of Molecular Biology, 1982
- Refinement of large structures by simultaneous minimization of energy and R factorActa Crystallographica Section A, 1978
- Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate.Proceedings of the National Academy of Sciences, 1978
- Regulation of aspartate carbamoyltransferase of Escherichia coli by the interrelationship of magnesium and nucleotidesBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Evidence from 13C NMR for protonation of carbamyl-P and N-(phosphonacetyl)-L-aspartate in the active site of aspartate transcarbamylase.Journal of Biological Chemistry, 1976
- Aspartate TranscarbamylaseJournal of Biological Chemistry, 1971