期刊
NATURE CHEMICAL BIOLOGY
卷 10, 期 1, 页码 50-U85出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1385
关键词
-
资金
- Schweizerische Nationalfonds-Ambizione grant [PZ00P3_136828/1]
- ETH fellowship
- Swiss National Science Foundation (SNF) [PZ00P3_136828] Funding Source: Swiss National Science Foundation (SNF)
The pyridine nucleotides NADH and NADPH (NAD(P)H) are ubiquitous redox coenzymes that are present in all living cells. Although about 16% of all characterized enzymes use pyridine nucleotides as hydride donors or acceptors during catalysis, a detailed understanding of how the hydride is transferred between NAD(P) H and the corresponding substrate is lacking for many enzymes. Here we present evidence for a new mechanism that operates during enzymatic hydride transfers using crotonyl-CoA carboxylase/reductase (Ccr) as a case study. We observed a covalent ene intermediate between NADPH and the substrate, crotonyl-CoA, using NMR, high-resolution MS and stopped-flow spectroscopy. Preparation of the ene intermediate further allowed direct access to the catalytic cycle of other NADPH-dependent enzymes-including those from type II fatty acid biosynthesis-in an unprecedented way, suggesting that formation of NAD(P) H ene intermediates is a more general principle in catalysis.
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。
推荐
暂无数据