| Title : Kinetic parameters of cholinesterase interactions with organophosphates: retrieval and comparison tools available through ESTHER database: ESTerases, alpha\/beta Hydrolase Enzymes and Relatives - Chatonnet_1999_Chem.Biol.Interact_119-120_567 |
| Author(s) : Chatonnet A , Hotelier T , Cousin X |
| Ref : Chemico-Biological Interactions , 119-120 :567 , 1999 |
| Abstract : Cholinesterases are targets for organophosphorus compounds which are used as insecticides, chemical warfare agents and drugs for the treatment of disease such as glaucoma, or parasitic infections. The widespread use of these chemicals explains the growing of this area of research and the ever increasing number of sequences, structures, or biochemical data available. Future advances will depend upon effective management of existing information as well as upon creation of new knowledge. The ESTHER database goal is to facilitate retrieval and comparison of data about structure and function of proteins presenting the alpha/beta hydrolase fold. Protein engineering and in vitro production of enzymes allow direct comparison of biochemical parameters. Kinetic parameters of enzymatic reactions are now included in the database. These parameters can be searched and compared with a table construction tool. ESTHER can be reached through internet (http://www.ensam.inra.fr/cholinesterase). The full database or the specialised X-window Client-server system can be downloaded from our ftp server (ftp://ftp.toulouse.inra.fr./pub/esther). Forms can be used to send updates or corrections directly from the web. |
| ESTHER : Chatonnet_1999_Chem.Biol.Interact_119-120_567 |
| PubMedSearch : Chatonnet_1999_Chem.Biol.Interact_119-120_567 |
| PubMedID: 10421496 |
Chatonnet A, Hotelier T, Cousin X (1999)
Kinetic parameters of cholinesterase interactions with organophosphates: retrieval and comparison tools available through ESTHER database: ESTerases, alpha\/beta Hydrolase Enzymes and Relatives
Chemico-Biological Interactions
119-120 :567
Chatonnet A, Hotelier T, Cousin X (1999)
Chemico-Biological Interactions
119-120 :567