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;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.
COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1
717
719
Stenta, Marco; Calvaresi, Matteo; Altoè, P.; Spinelli, Domenico; Garavelli, Marco; Bottoni, Andrea
File in questo prodotto:
Eventuali allegati, non sono esposti

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11585/59877
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 0
  • ???jsp.display-item.citation.isi??? 0
social impact