Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5261483 | Tetrahedron Letters | 2014 | 6 Pages |
Abstract
McbA was characterized in vitro as a novel amide synthetase in the marinacarbolines A-D biosynthetic pathway, catalyzing amide bond formation between 1-acetyl-3-carboxy-β-carboline (1a) and substituted-β-phenethylamines (1b, 2b, 3b) and tryptamine (4b) in an ATP-dependent manner. Enzyme kinetic analyses highlight β-phenethylamine as the most suitable amine donor. McbA showed broad substrate compatibility with substituted amines; 10 new β-carboline analogues were chemoenzymatically generated.
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Organic Chemistry
Authors
Changtao Ji, Qi Chen, Qinglian Li, Hongbo Huang, Yongxiang Song, Junying Ma, Jianhua Ju,