4.8 Article

The pathway for coenzyme M biosynthesis in bacteria

出版社

NATL ACAD SCIENCES
DOI: 10.1073/pnas.2207190119

关键词

Xanthobacter autotrophicus; CoM biosynthesis; aspartase/fumarase superfamily; sulfonate; PLP-dependent cysteine desulfhydrase

资金

  1. US Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences [DE-SC0018143]
  2. United States Department of Agriculture National Institute of Food and Agriculture [15621]
  3. M.J. Murdock Charitable Trust [SR-201912845]
  4. DOE [DE-AC36-08GO28308]
  5. US DOE Office of Science Early Career Program
  6. U.S. Department of Energy (DOE) [DE-SC0018143] Funding Source: U.S. Department of Energy (DOE)

向作者/读者索取更多资源

The article introduces the complete CoM biosynthesis pathway in bacteria, revealing distinct chemical steps compared to CoM biosynthesis in methanogenic archaea, which represents a profound instance of convergent evolution.
Mercaptoethane sulfonate or coenzyme M (CoM) is the smallest known organic cofactor and is most commonly associated with the methane-forming step in all methanogenic archaea but is also associated with the anaerobic oxidation of methane to CO2 in anaerobic methanotrophic archaea and the oxidation of short-chain alkanes in Syntrophoarchaeum species. It has also been found in a small number of bacteria capable of the metabolism of small organics. Although many of the steps for CoM biosynthesis in methanogenic archaea have been elucidated, a complete pathway for the biosynthesis of CoM in archaea or bacteria has not been reported. Here, we present the complete CoM biosynthesis pathway in bacteria, revealing distinct chemical steps relative to CoM biosynthesis in methanogenic archaea. The existence of different pathways represents a profound instance of convergent evolution. The five-step pathway involves the addition of sulfite, the elimination of phosphate, decarboxylation, thiolation, and the reduction to affect the sequential conversion of phosphoenolpyruvate to CoM. The salient features of the pathway demonstrate reactivities for members of large aspartase/fumarase and pyridoxal 5'-phosphate-dependent enzyme families.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据