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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gerhart, John |
| Description | Country affiliation: United States Author Affiliation: Gerhart J ( Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.) |
| Abstract | Aspartate transcarbamoylase (ATCase) of Escherichia coli, the first enzyme of the pyrimidine biosynthetic pathway, is inhibited by CTP and UTP, the nucleotide end-products of the pathway. First discovered by Yates and Pardee in 1956 [Yates R & Pardee AB (1956) J Biol Chem 221, 743-756; Yates RA & Pardee AB (1956) J Biol Chem 221, 757-770], these interactions establish feedback inhibition in vivo, a key means of metabolic regulation by which end-product production by the pathway is adjusted to end-product usage in macromolecule synthesis. Activation of the enzyme by the purine nucleotide ATP may also have regulatory significance. ATCase and threonine deaminase of E. coli were the first enzymes to be characterized with regard to their allosteric properties, namely, sigmoidal saturation with regard to substrates, reflecting cooperative ligand binding at the active site, and inhibition and activation by nucleotides of very different chemical structure from the substrates. In the case of ATCase, the nucleotides bind at regulatory sites located on protein subunits different from those bearing the active sites. The early characterization of ATCase proved useful in the 1965 conceptualization of the allosteric transition by Monod, Wyman, and Changeux [Monod J et al. (1965) J Mol Biol 12, 88-118], and the protein in subsequent years has proved useful in the experimental analysis of the interactions of sites and of conformational changes in allosteric proteins. This is an account of the early years of work on ATCase, up to 1965. |
| File Format | HTM / HTML |
| ISSN | 1742464X |
| Issue Number | 2 |
| Volume Number | 281 |
| e-ISSN | 17424658 |
| Journal | FEBS Journal |
| Language | English |
| Publisher | Wiley (on behalf of the Federation of European Biochemical Societies) |
| Publisher Date | 2014-01-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Aspartate Carbamoyltransferase Chemistry Escherichia Coli Proteins Escherichia Coli Enzymology Allosteric Regulation Allosteric Site Metabolism Feedback, Physiological Kinetics Models, Biological Models, Chemical Protein Binding Protein Subunits Journal Article Review |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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