IS CHORISMATE MUTASE A PROTOTYPIC ENTROPY TRAP - ACTIVATION PARAMETERS FOR THE BACILLUS-SUBTILIS ENZYME

Authors
KAST P ASIFULLAH M HILVERT D
Citation
P. Kast et al., IS CHORISMATE MUTASE A PROTOTYPIC ENTROPY TRAP - ACTIVATION PARAMETERS FOR THE BACILLUS-SUBTILIS ENZYME, Tetrahedron letters, 37(16), 1996, pp. 2691-2694
Citations number
30
Categorie Soggetti
Chemistry Inorganic & Nuclear
Journal title
Tetrahedron letters → ACNP
ISSN journal
00404039
Volume
37
Issue
16
Year of publication
1996
Pages
2691 - 2694
Database
ISI
SICI code
0040-4039(1996)37:16<2691:ICMAPE>2.0.ZU;2-M
Abstract
Chorismate mutase is thought to accelerate the chorismate-to-prephenat e rearrangement in part by significantly lowering the entropy barrier for the reaction. We have determined the activation parameters for the well-characterized Bacillus subtilis chorismate mutase and find that Delta S double dagger (-9.1 +/- 1.2 eu) is nearly as unfavorable as th e activation entropy for the uncatalyzed process. Our results suggest that chorismate mutase catalysts show greater mechanistic versatility than commonly believed. Copyright (C) 1996 Elsevier Science Ltd.