期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 21, 期 24, 页码 7321-7324出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2011.10.026
关键词
Monoacylglycerol lipase; 2-Arachidonoylglycerol; Benzisothiazolinone; Octhilinone; Cysteine
资金
- UCL (Universite Catholique de Louvain)
- F.R.S.-FNRS (Fonds de la Recherche Scientifique, Belgium) [2.4604.09, 3.4552.11]
- Inter-university Attraction Pole program [IAP P6/P19 PROFUSA]
The regulation of 2-arachidonoylglycerol (2-AG) levels is a major issue as 2-AG has been proven to participate in numerous physiopathological phenomena such as neuroprotection or analgesia. Octhilinone, a cysteine-reagent compound, has recently been shown to inhibit in the nanomolar range monoacylglycerol lipase (MAGL), the major enzyme responsible for the degradation of 2-AG. Here, we further investigate the mechanism by which octhilinone and its benzisothiazolinone analog inhibit human MAGL. We also provide new information on the structural requirements for MAGL inhibition by these compounds. Finally, we describe for N-octylbenzisothiazolinone a mode of inhibition which is partially different from that described for octhilinone, especially with regard to the targeted cysteine residues in the vicinity of the catalytic site. (C) 2011 Elsevier Ltd. All rights reserved.
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