Characterization of S-Ribosylhomocysteinase (LuxS): Mechanism and Inhibition - Couverture souple

Zhu, Jinge

 
9783639165159: Characterization of S-Ribosylhomocysteinase (LuxS): Mechanism and Inhibition
Couverture souple
ISBN 10 : 3639165152 ISBN 13 : 9783639165159
Editeur : VDM Verlag, 2009

Synopsis

S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine to produce L- homocysteine and 4,5-dihydroxy-2,3-pentanedione, the precursor of type II bacterial quorum sensing autoinducer. This work carried out extensive mechanistic studies of the LuxS reaction. The native metal cofactor of LuxS was identified as ferrous ion, instead of previously reported zinc ion, with a potential catalytic role. Substantial evidence was provided for the internal redox reaction, which comprised two consecutive carbonyl migration steps followed by ?-elimination. Three LuxS activity assays were developed and greatly facilitated the mechanistic investigations of LuxS. Two classes of LuxS inhibitors were designed based on metal chelation and catalytic mechanism, respectively. They encouraged future development of LuxS inhibitors as novel antibacterial agents and helped probe the catalytic mechanism of LuxS.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine to produce L- homocysteine and 4,5-dihydroxy-2,3-pentanedione, the precursor of type II bacterial quorum sensing autoinducer. This work carried out extensive mechanistic studies of the LuxS reaction. The native metal cofactor of LuxS was identified as ferrous ion, instead of previously reported zinc ion, with a potential catalytic role. Substantial evidence was provided for the internal redox reaction, which comprised two consecutive carbonyl migration steps followed by ?-elimination. Three LuxS activity assays were developed and greatly facilitated the mechanistic investigations of LuxS. Two classes of LuxS inhibitors were designed based on metal chelation and catalytic mechanism, respectively. They encouraged future development of LuxS inhibitors as novel antibacterial agents and helped probe the catalytic mechanism of LuxS.

Biographie de l'auteur

Jinge Zhu Ph.D., Biochemistry, The Ohio State University, Columbus, OH (2005); Research Associate, University of Wisconsin - Madison.

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
VDM Verlag
Date d'édition
2009
Langue
anglais
ISBN 10 
3639165152
ISBN 13 
9783639165159
Reliure
Broché
Nombre de pages
224
Coordonnées du fabricant
non disponible
Personne responsable
non disponible