The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme
AUTOR(ES)
Hur, Sun
FONTE
The National Academy of Sciences
RESUMO
Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic interactions with TS are much weaker than with chorismate. Interactions and the mechanism of catalysis of chorismate → prephenate by the EcCM enzyme are discussed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=122163Documentos Relacionados
- Genetic separability of the chorismate mutase and prephenate dehydrogenase components of the Escherichia coli tyrA gene product.
- Phenylalanine Biosynthesis in Escherichia coli K-12: Mutants Derepressed for Chorismate Mutase P-Prephenate Dehydratase
- Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus.
- Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus.
- The near attack conformation approach to the study of the chorismate to prephenate reaction
