Multiple C-C Bond Cleavage Reactions Catalyzed by Tolyporphin Tetrapyrrole Biosynthetic Enzymes
Multiple C-C Bond Cleavage Reactions Catalyzed by Tolyporphin Tetrapyrrole Biosynthetic Enzymes
复制标题
Tolyporphin 四吡咯生物合成酶催化的多重 C-C 键断裂反应
DOI：
10.1021/jacs.3c01993
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发表时间：
2023
影响因子：
15
通讯作者：
Ikuro Abe
中科院分区：
文献类型：
--
作者：
Richiro Ushimaru;Jiaqi Lyu;Meiqi Ling;Ikuro Abe
卟啉A是一种罕见的四吡咯次生代谢物，含有悬垂的脱氧糖和未取代的吡咯β位点。在这里，我们描述了生物合成的多肽苷核。HemF1催化了血红素生物合成的中间体卟啉原III的两个丙酸侧链的氧化脱羧。然后HemF2处理剩下的两个丙酸基团生成四烯基中间体。TolI通过重复的C-C键切割截断了大环上的所有四个乙烯基，生成了卟啉的未取代吡咯β位点。这项研究说明了前所未有的C-C键裂解反应如何从典型血红素生物合成分支产生多卟啉。
Tolyporphin A is an unusual tetrapyrrole secondary metabolite containing pendant deoxysugars and unsubstituted pyrrole β sites. Herein, we describe the biosynthesis of the tolyporphin aglycon core. HemF1 catalyzes the oxidative decarboxylation of two propionate side chains of coproporphyrinogen III, an intermediate in heme biosynthesis. HemF2 then processes the two remaining propionate groups to generate a tetravinyl intermediate. All four vinyl groups from the macrocycle are truncated by TolI via repeated C–C bond cleavages to generate the unsubstituted pyrrole β sites of tolyporphins. This study illustrates how the unprecedented C–C bond cleavage reactions branch from canonical heme biosynthesis to produce tolyporphins.