A QM/MM study has been carried out to clarify the catalytic mechanism of the enzyme diaminopimelate (DAP) epimerase. In particular the potential energy surface (PES) for the stereo‐inversion of the distal Cα of the substrate has been has been investigated. The nature of the critical points located on the PES has been checked by numerical frequencies calculations. The role of the various aminoacid residues in the catalysis has been elucidated using a recently developed analysis method.
The Catalytic Activity of Diaminopimelate Epimerase: a QM/MM Study / Stenta, Marco; Calvaresi, Matteo; Altoè, P.; Spinelli, Domenico; Garavelli, Marco; Bottoni, Andrea. - STAMPA. - 963:(2007), pp. 717-719. (Intervento presentato al convegno International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007) tenutosi a Corfu (Greece) nel 25–30 SEPTEMBER 2007) [10.1063/1.2836189].
The Catalytic Activity of Diaminopimelate Epimerase: a QM/MM Study
STENTA, MARCO;CALVARESI, MATTEO;SPINELLI, DOMENICO;GARAVELLI, MARCO;BOTTONI, ANDREA
2007
Abstract
A QM/MM study has been carried out to clarify the catalytic mechanism of the enzyme diaminopimelate (DAP) epimerase. In particular the potential energy surface (PES) for the stereo‐inversion of the distal Cα of the substrate has been has been investigated. The nature of the critical points located on the PES has been checked by numerical frequencies calculations. The role of the various aminoacid residues in the catalysis has been elucidated using a recently developed analysis method.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
