Kinetics of aspartate transcarbamylase from Escherichia coli for the reverse direction of reaction.
Open Access
- 1 November 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (22) , 11428-11433
- https://doi.org/10.1016/s0021-9258(19)68417-6
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Effect of pH on local and gross conformational changes in aspartate transcarbamylaseBiochemical and Biophysical Research Communications, 1980
- E. coli aspartate transcarbamylase: Part II: Structure and allosteric interactionsTrends in Biochemical Sciences, 1980
- E. coli aspartate transcarbamylase: Part I: Catalytic and regulatory functionsTrends in Biochemical Sciences, 1980
- Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state modelBiochemistry, 1977
- Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunitsBiochemistry, 1977
- Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog N-(phosphonacetyl)-L-aspartateBiochemistry, 1977
- Aspartate transcarbamylase from Streptococcus faecalis. Reverse reaction and binding studiesBiochemistry, 1974
- Kinetic analysis of coupled enzyme assaysBiochemistry, 1969
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic MercurialsJournal of the American Chemical Society, 1954