Gibbs free energy for intramolecular rearrangement of chorismate to prephenate

Range -56±9 kJ/mol
Organism Bacteria Bacillus subtilis
Reference Mattei P, Kast P, Hilvert D. Bacillus subtilis chorismate mutase is partially diffusion-controlled. Eur J Biochem. 1999 Apr261(1):25-32. p.25 left columnPubMed ID10103029
Primary Source Peter Kast , Yadu B. Tewari , Olaf Wiest , Donald Hilvert , Kendall N. Houk , and Robert N. Goldberg, Thermodynamics of the Conversion of Chorismate to Prephenate:? Experimental Results and Theoretical Predictions, J. Phys. Chem. B, 1997, 101 (50), pp 10976–10982 DOI: 10.1021/jp972501l
Comments "The intramolecular rearrangement of chorismate to prephenate is the first committed step in the biosynthesis of phenylalanine and tyrosine [1]. As a rare example of a biological pericyclic process, this reaction has been the subject of much study. It is strongly exergonic (?Gr =-56±9kJ/mol at 298 K) [primary source] and occurs spontaneously at an appreciable rate by a concerted but asynchronous pathway [3,4]"
Entered by Uri M
ID 109297