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Kinetic Studies with Rat-Brain Succinic-Semialdehyde Dehydrogenase
| Content Provider | Scilit |
|---|---|
| Author | Rivett, A. Jennifer Tipton, Keith F. |
| Copyright Year | 2005 |
| Description | Journal: Journal of Biological Inorganic Chemistry A simple procedure is described that gives an approximately 100-fold purification of rat brain succinic-semialdehyde dehydrogenase with a high yield. The enzyme exhibits a relatively low Km value for succinic semialdehyde (2.5 microM) and is inhibited by high concentrations of that substrate in an uncompetitive manner with respect to NAD+ (Ki = 150 microM). p-Hydroxybenzaldehyde was shown to give competitive inhibition with respect to succinic semialdehyde and uncompetitive inhibition with respect to NAD+. Initial rate studies in the presence of a fixed concentration of this inhibitor allowed a more accurate estimation of the kinetic parameters for the uninhibited reaction. The results of these studies, together with analysis of the dead-end inhibition by AMP and the effects of NAD+ and 3-acetylpyridine--adenine dinucleotide as alternative acceptors in the reaction, were consistent with the enzyme-catalysed reaction obeying a compulsory-order mechanism in which NAD+ was the first substrate to bind to the enzyme and NADH was the last product to dissociate from it. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1981.tb06319.x/pdf |
| Ending Page | 193 |
| Page Count | 7 |
| Starting Page | 187 |
| ISSN | 09498257 |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1981.tb06319.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 1 |
| Volume Number | 117 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2005-03-03 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Succinic Semialdehyde |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
