Unusual non-enzymatic flavin catalysis enhances understanding of flavoenzymes

Unusual non-enzymatic flavin catalysis enhances understanding of flavoenzymes
复制标题

DOI:
10.1016/j.febslet.2015.02.034
复制
发表时间:
2015-04-02
期刊:
影响因子:
3.5
通讯作者:
Schneider, Tanya L.
Schneider, Tanya L.
中科院分区:
生物学3区
文献类型:
--
作者:
Argueta, Erick A.;Amoh, Amanda N.;Schneider, Tanya L.

文献摘要

被引文献

相似文献

黄素辅因子是许多生化转化的中心,通常作为催化活性黄素酶的一部分紧密结合在一起。这项工作表明,天然黄素可以作为单独的催化剂,在水溶液中促进生物合成激发的杂环的氧化。黄素活性与非核糖体肽合成中重要的氧化酶的活性进行了比较,提供了单独使用黄素和在完整黄素酶的情况下进行催化效率的罕见的直接比较。这项研究表明,这类氧化酶很可能具有活性部位的碱基,因为氧化酶的活性高于单独的黄素,特别是对于酸性较弱的底物。这些发现为开发健壮的、催化有效的、设计的微型黄素酶提供了前景。(C)2015年欧洲生化学会联合会。爱思唯尔出版,版权所有。
Flavin cofactors are central to many biochemical transformations and are typically tightly bound as part of a catalytically active flavoenzyme. This work indicates that naturally occurring flavins can act as stand-alone catalysts to promote the oxidation of biosynthetically inspired heterocycles in aqueous buffers. Flavin activity was compared with that of oxidases important in non-ribosomal peptide synthesis, providing a rare direct comparison between the catalytic efficacy of flavins alone and in the context of a full flavoenzyme. This study suggests that such oxidases are likely to possess an active site base, as oxidase activity was greater than that of flavins alone, particularly for less acidic substrates. These findings offer perspective on the development of robust and catalytically effective, designed miniature flavoenzymes. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.