22712-32-9Relevant academic research and scientific papers
Isolation of a novel protein tyrosine phosphatase inhibitor, 2-methyl-fervenulone, and its precursors from Streptomyces
Wang,Kah Leong Lim,Su Ling Yeo,Xu,Mui Mui Sim,Ting,Wang,Yee,Tan,Pallen
, p. 1641 - 1646 (2000)
High-throughput screening identified an extract from Streptomyces sp. IM 2096 with inhibitory activity toward several protein tyrosine phosphatases (PTPs). Four 1,2,4-triazine compounds 2096A-D (1-4) were isolated from this extract and their structures elucidated by interpretation of spectroscopic data and confirmed by degradation and synthesis. The novel glycocyamidine derivatives 1 and 2 are diastereomers and may interconvert. Both are inactive in the PTP inhibition assay. Compounds 1 and 2 are unstable and partially decompose to 3 and glycocyamidine (5) at room temperature. Compound 3, known as MSD-92 or 2-methyl-fervenulone, is a broad-specificity PTP inhibitor with comparable potency to vanadate. The imidazo[4,5-e]-1,2,4-triazine (4), inactive in the PTP-inhibition assay, may be a degradation product of 3.
