The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide.
The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide.
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DOI：
10.1021/acs.biochem.6b00355
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发表时间：
2016-05-24
期刊：
影响因子：
2.9
通讯作者：
Bandarian V
中科院分区：
文献类型：
--
作者：
Bruender NA;Bandarian V
核糖体合成的后修饰肽，RIPPs，在各种微生物的基因组中编码，与编码进行广泛修饰的酶的ORF非常接近，其中许多是新的。最近，自由基S-腺苷-L-甲硫氨酸（SAM）超家族的成员已被确定在这些生物合成集群。在本文中，我们证明了假定的自由基SAM酶，MftC，氧化脱羧的辅助蛋白MftB的存在下的MftA肽的C-末端。由MftC催化的反应扩展了分子内交联之外的基于肽的自由基SAM化学的所有组成部分。
Ribosomally-synthesized post-translationally modified peptides, RiPPs, are encoded in the genomes of a wide variety of microorganisms, in close proximity to orfs that encode enzymes that carry out extensive modifications, many of which are novel. Recently, members of the radical S-adenosyl-l-methionine (SAM) superfamily have been identified in these biosynthetic clusters. Herein we demonstrate the putative radical SAM enzyme, MftC, oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. The reaction catalyzed by MftC expands the repertoire of peptide-based radical SAM chemistry beyond the intramolecular crosslinks.