Related Content
Search Google Scholar for:
|
|
Science 5 August 1988:
Vol. 241. no. 4866, pp. 669 - 674
DOI: 10.1126/science.3041592
|
|
Articles
Science, Vol 241, Issue 4866, 669-674
Copyright © 1988 by American Association for the Advancement of Science
Escherichia coli aspartate transcarbamylase: the relation between structure and function
ER Kantrowitz
and
WN Lipscomb
Department of Chemistry, Boston College, MA 02167.
The x-ray structures of the allosteric enzyme aspartate transcarbamylase from Escherichia coli have been solved and refined for both allosteric forms. The T form was determined in the presence of the heterotropic inhibitor cytidine triphosphate, CTP, while the R form was determined in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate. These two x-ray structures provide the starting point for an understanding of how allosteric enzymes are able to control the rates of metabolic pathways. Insights into the mechanisms of both catalysis and homotropic cooperativity have been obtained by using site-directed mutagenesis to probe residues thought to be critical to the function of the enzyme based on these x-ray structures.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein gp140 and Escherichia coli Aspartate Transcarbamoylase.
- B. Chen, Y. Cheng, L. Calder, S. C. Harrison, E. L. Reinherz, J. J. Skehel, and D. C. Wiley (2004)
J. Virol.
78, 4508-4516
| Abstract »
| Full Text »
| PDF »
- A Fluorescent Probe-labeled Escherichia coli Aspartate Transcarbamoylase That Monitors the Allosteric Conformational State.
- J. M. West, H. Tsuruta, and E. R. Kantrowitz (2004)
J. Biol. Chem.
279, 945-951
| Abstract »
| Full Text »
| PDF »
- Aquifex aeolicus Aspartate Transcarbamoylase, an Enzyme Specialized for the Efficient Utilization of Unstable Carbamoyl Phosphate at Elevated Temperature.
- C. Purcarea, A. Ahuja, T. Lu, L. Kovari, H. I. Guy, and D. R. Evans (2003)
J. Biol. Chem.
278, 52924-52934
| Abstract »
| Full Text »
| PDF »
- The Role of Intersubunit Interactions for the Stabilization of the T State of Escherichia coli Aspartate Transcarbamoylase.
- R. S. Chan, J. B. Sakash, C. P. Macol, J. M. West, H. Tsuruta, and E. R. Kantrowitz (2002)
J. Biol. Chem.
277, 49755-49760
| Abstract »
| Full Text »
| PDF »
- Stabilization of the R Allosteric Structure of Escherichia coli Aspartate Transcarbamoylase by Disulfide Bond Formation.
- J. M. West, H. Tsuruta, and E. R. Kantrowitz (2002)
J. Biol. Chem.
277, 47300-47304
| Abstract »
| Full Text »
| PDF »
- Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.
- L. Fetler, P. Tauc, D.P. Baker, C.P. Macol, E.R. Kantrowitz, and P. Vachette (2002)
Protein Sci.
11, 1074-1081
| Abstract »
| Full Text »
| PDF »
- Allosteric Regulation of Catalytic Activity: Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate Mutase.
- K. Helmstaedt, S. Krappmann, and G. H. Braus (2001)
Microbiol. Mol. Biol. Rev.
65, 404-421
| Abstract »
| Full Text »
| PDF »
- Transition state structure of arginine kinase: Implications for catalysis of bimolecular reactions.
- G. Zhou, T. Somasundaram, E. Blanc, G. Parthasarathy, W. R. Ellington, and M. S. Chapman (1998)
PNAS
95, 8449-8454
| Abstract »
| Full Text »
| PDF »
- Engineered Complementation in Escherichia coli Aspartate Transcarbamoylase. HETEROTROPIC REGULATION BY QUATERNARY STRUCTURE STABILIZATION.
- J. M. Aucoin, E. J. Pishko, D. P. Baker, and E. R. Kantrowitz (1996)
J. Biol. Chem.
271, 29865-29869
| Abstract »
| Full Text »
| PDF »
- Domain Closure in the Catalytic Chains of Escherichia coli Aspartate Transcarbamoylase Influences the Kinetic Mechanism.
- B. H. Lee, B. W. Ley, E. R. Kantrowitz, M. H. O'Leary, and F. C. Wedler (1995)
J. Biol. Chem.
270, 15620-15627
| Abstract »
| Full Text »
| PDF »
- L-Aspartate Association Contributes to Rate Limitation and Induction of the T [IMAGE] R Transition in Escherichia coli Aspartate Transcarbamoylase.
- F. C. Wedler, B. W. Ley, B. H. Lee, M. H. O'Leary, and E. R. Kantrowitz (1995)
J. Biol. Chem.
270, 9725-9733
| Abstract »
| Full Text »
| PDF »
- Characterization of the Aspartate Transcarbamoylase from Methanococcus jannaschii.
- E. S. Hack, T. Vorobyova, J. B. Sakash, J. M. West, C. P. Macol, G. Herve, M. K. Williams, and E. R. Kantrowitz (2000)
J. Biol. Chem.
275, 15820-15827
| Abstract »
| Full Text »
| PDF »
|
|
