Co-operative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase: Role of the C-terminal region of the regulatory chains
- 20 November 1990
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 216 (2), 375-384
- https://doi.org/10.1016/s0022-2836(05)80328-6
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Escherichia coli Aspartate Transcarbamoylase: Structure, Energetics, and Catalytic and Regulatory MechanismsAnnual Review of Biophysics, 1989
- Complex of N-phosphonacetyl-l-aspartate with aspartate carbamoyltransferaseJournal of Molecular Biology, 1988
- 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-l-aspartateJournal of Molecular Biology, 1987
- The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: A molecular modelling studyBiochemical and Biophysical Research Communications, 1987
- Homotropic effects in aspartate transcarbamoylaseJournal of Molecular Biology, 1985
- Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scatteringJournal of Molecular Biology, 1985
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coliJournal of Molecular Biology, 1982
- Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transitionJournal of Molecular Biology, 1979
- Biosynthesis of Escherichia coli aspartate transcarbamylase: I. Parameters of gene expression and sequential biosynthesis of the subunitsJournal of Molecular Biology, 1972