期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 384, 期 2, 页码 210-214出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.04.101
关键词
Ascorbic acid; Vitamin C; Erythroascorbic acid; Ubiquitin
资金
- Japan Science and Technology Agency
We recently identified a microbial conversion of L-ascorbic acid (AsA) to L-erythroascorbic acid (eAsA), a five-carbon analog of AsA. In this paper, we show that ubiquitin plays a crucial role in this process. Based on an assay that determined AsA decomposition, we purified proteins that had N-terminal amino acid sequences identical to that of yeast ubiquitin. Purified ubiquitin facilitated decompositions of AsA and dehydro-AsA, accompanying a partial conversion to eAsA through Cl-elimination. Acetylation or limited hydrolysis of ubiquitin abolished its activity. A mutant ubiquitin, with Lys(6) replaced by Arg, completely lost activity, whereas a mutant, with six other Lys residues (positions at 11, 27, 29, 33, 48 and 63) substituted by Arg, retained activity. Thus, Lys(6), Which locates in close proximity to H is crucial for ubiquitin activity in the AsA conversion to eAsA. (C) 2009 Elsevier Inc. All rights reserved.
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