紫红色杆菌
吲哚试验
生物化学
酶
化学
色氨酸
生物合成
血红素
大肠杆菌
立体化学
代谢物
氨基酸
群体感应
毒力
基因
作者
Carl J. Balibar,Christopher T. Walsh
出处
期刊:Biochemistry
[American Chemical Society]
日期:2006-12-01
卷期号:45 (51): 15444-15457
被引量:149
摘要
The purple chromobacterial pigment violacein arises by enzymatic oxidation and coupling of two molecules of l-tryptophan to give a rearranged pyrrolidone-containing scaffold in the final pigment. We have purified five contiguously encoded proteins VioA−E after expression in Escherichia coli and demonstrate the full 14-electron oxidation pathway to yield the final chromophore. The flavoenzyme VioA and the heme protein VioB work in conjunction to oxidize and dimerize l-tryptophan to a nascent product that can default to the off pathway metabolite chromopyrrolic acid. In the presence of VioE, the intermediate instead undergoes on-pathway [1,2] indole rearrangement to prodeoxyviolacein. The last two enzymes in the pathway are flavin-dependent oxygenases, VioC and VioD, that act sequentially. VioD hydroxylates one indole ring at the 5-position to yield proviolacein, and VioC then acts on the other indole ring at the 2-position to create the oxindole and complete violacein formation.
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