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The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K-12. Incubation of the Enzyme in Alkaline Conditions: Dissociation and Disulfide-Bridge Formation
| Content Provider | Scilit |
|---|---|
| Author | Jacques, Yannick Truffa‐Bachi, Paolo |
| Copyright Year | 1976 |
| Description | Journal: Journal of Biological Inorganic Chemistry Aspartokinase I - homoserine dehydrogenase I from Escherichia coli K-12, a homotetrameric enzyme, dissociates into dimers upon alkaline treatment. Both aspartokinase and homoserine dehydrogenase inactivation, as well as desensitazion towards L-threonine, occur in a multi-step process. Dithiothreitol stabilizes a dimeric form retaining full activity and sensitivity; L-homoserine stabilizing another dimeric form devoid of aspartokinase activity and retaining a substantial dehydrogenase activity insensitive toward L-threonine. A model is proposed showing that dissociation into dimers occurs in a first step, the resulting dimer losing both aspartokinase and homoserine dehydrogenase sensitivity in two subsequent steps involving the formation of intrachain disulfide bonds. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1976.tb10182.x/pdf |
| Ending Page | 490 |
| Page Count | 6 |
| Starting Page | 485 |
| ISSN | 09498257 |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1976.tb10182.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 3 |
| Volume Number | 62 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1976-03-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Homoserine Dehydrogenase Escherichia Coli Coli K Disulfide Bridge Bridge Formation Threonine Sensitive Sensitive Homoserine Aspartokinase Activities |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |