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Phosphoserine Aminotransferase, the Second Step-Catalyzing Enzyme for Serine Biosynthesis
| Content Provider | Scilit |
|---|---|
| Author | Basurko, Marie-Jose Marche, Michele Darriet, Monique Cassaigne, Andre |
| Copyright Year | 1999 |
| Description | As a step toward analyzing the serine biosynthetic pathway in mammals, we have studied the properties of phosphoserine aminotransferase, the second step‐catalyzing enzyme. The Km values for 3‐phosphohydroxypyruvate and L‐phosphoserine are 5 and 35 mu M, respectively, and those for glutamate and alpha‐ketoglutarate are 1.2 and 0.8 mM, respectively. The product inhibition studies strengthened the support for a ping‐pong mechanism and allowed evaluation of Ki values for the four substrates. The equilibrium constant evaluated from the kinetic parameters is 40. Additionally, some physical properties relative to the bound coenzyme and the secondary structure were investigated. The results are consistent with a structural relationship between the Escherichia coli enzyme and the mammalian enzyme. The mammalian enzyme has specific kinetic parameters, the determination of which is a prerequisite to analyzing the serine biosynthetic pathway in mammals. |
| Related Links | https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1080/713803557 |
| Ending Page | 529 |
| Page Count | 5 |
| Starting Page | 525 |
| e-ISSN | 15216551 |
| DOI | 10.1080/713803557 |
| Journal | IUBMB life |
| Issue Number | 5 |
| Volume Number | 48 |
| Language | English |
| Publisher | Informa UK Limited |
| Publisher Date | 1999-11-01 |
| Access Restriction | Open |
| Subject Keyword | Biophysics Phosphoserine Aminotransferase Pyridoxal Phosphatedependent Enzyme Serine Biosynthesis |
| Content Type | Text |
| Resource Type | Article |
