The isolation and structure elucidation of YM-254890, a novel Gq/11 inhibitor from Chromobacterium sp. QS3666, is described. The gross structure was determined by one- and two-dimensional NMR studies and mass spectrometry. YM-254890 is a cyclic depsipeptide containing uncommon amino acids; β-hydroxyleucine (two residues), N,O-dimethylthreonine and N-methyldehydroalanine. YM-254890 exists as a mixture of two conformers in a variety of NMR solvents, and the distinction between major and minor conformers appears to lie in the geometry of the amide bond between 3-phenyllactic acid and N-methyldehydroalanine. The absolute stereochemistery was elucidated by Marfey's analysis and chiral HPLC analysis of the acid hydrolysate of YM-254890. © 2003 Elsevier Science Ltd. All rights reserved.
CITATION STYLE
Taniguchi, M., Suzumura, K. I., Nagai, K., Kawasaki, T., Saito, T., Takasaki, J., … Tsukamoto, S. I. (2003). Structure of YM-254890, a novel Gq/11 inhibitor from Chromobacterium sp. QS3666. Tetrahedron, 59(25), 4533–4538. https://doi.org/10.1016/S0040-4020(03)00680-X
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