| Literature DB >> 31860798 |
Guillem Pons1, Daniel Riba1, Mireia Casasampere1,2, Eduardo Izquierdo1,2, José-Luís Abad1, Gemma Fabriàs1,3, Pilar G Rodríguez Ortega4, Juan J López-González4, Manuel Montejo4, Josefina Casas1,3, Antonio Delgado1,2.
Abstract
The synthesis of a series of vinylated analogues of sphingosine-1-phosphate together with their unambiguous configurational assignment by VCD methods is reported. Among them, compound RBM10-8 can irreversibly inhibit human sphingosine-1-phosphate lyase (hS1PL) while behaving also as an enzyme substrate. These findings, together with the postulated mechanism for S1PL activity, reinforce the role of RBM10-8 as a new mechanism-based hS1PL inhibitor.Entities:
Year: 2020 PMID： 31860798 DOI： 10.1021/acs.joc.9b02420
Source DB: PubMed Journal: J Org Chem ISSN： 0022-3263 Impact factor: 4.354