Pomponi_1998_Biophys.Chem_72_239

Reference

Title : The role of TRP84 in catalytic power and the specificity of AChE - Pomponi_1998_Biophys.Chem_72_239
Author(s) : Pomponi M , Sacchi S , Colella A , Patamia M , Marta M
Ref : Biophysical Chemistry , 72 :239 , 1998
Abstract :

The structure-function relationship between the alkaloids physostigmine, physovenine and the three structurally related compounds were investigated by employing kinetic studies and molecular modeling. Crystallographic data from the X-ray conformation of the Torpedo californica acetylcholinesterase complex together with the transition state analog inhibitor m-(N,N,N,-Trimethylammonio) trifluoroacetophenone (TMTFA) was used as template onto which inhibitors were superimposed. Among the structural elements of the active site, TRP84 residue shows a versatile role. In fact, its aromatic electrons not only can be employed in pi-cation interactions, as is the case for ACh, but they can also provide a polarizable surface for van der Waals and London interactions.

PubMedSearch : Pomponi_1998_Biophys.Chem_72_239
PubMedID: 9691268

Related information

Inhibitor Physovenine

Citations formats

Pomponi M, Sacchi S, Colella A, Patamia M, Marta M (1998)
The role of TRP84 in catalytic power and the specificity of AChE
Biophysical Chemistry 72 :239

Pomponi M, Sacchi S, Colella A, Patamia M, Marta M (1998)
Biophysical Chemistry 72 :239