## Abstract A cyclinβdependent kinase, Cdk2, catalyzes the transfer of the Ξ³βphosphate from ATP to a threonine or serine residue of its polypeptide substrates. Here, we investigate aspects of the reaction mechanism of Cdk2 by gasβphase density functional calculations, classical molecular dynamics,
β¦ LIBER β¦
The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study
β Scribed by Przemyslaw G Czyryca; Alvan C Hengge
- Book ID
- 114149012
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 800 KB
- Volume
- 1547
- Category
- Article
- ISSN
- 0167-4838
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While the process of the Ah receptor activation leading to cytochrome P450 induction has been well studied, the mechanism and the process through which the Ah receptor activates tyrosine kinases, within a few minutes of its ligand binding, is not known. Previously, it was reported by Tannheimer et a