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学科主题: 生命有机化学
题名: The structural basis of an NADP(+)-independent dithiol oxidase in FK228 biosynthesis
其他题名: The structural basis of an NADP(+)-independent dithiol oxidase in FK228 biosynthesis
作者: LI JIE; WANG CHENG; ZHANG ZHIMIN; CHENG YIQIANG; Zhou JH(周佳海)
刊名: Sci Rep
发表日期: 2014
DOI: 10.1038/srep04145
卷: 4, 页:4145
收录类别: SCI
英文摘要: The disulfide bond is unusual in natural products and critical for thermal stability, cell permeability and bioactivity. DepH from Chromobacterium violaceum No. 968 is an FAD-dependent enzyme responsible for catalyzing the disulfide bond formation of FK228, an anticancer prodrug approved for the treatment of cutaneous T-cell lymphoma. Here we report the crystal structures of DepH and DepH complexed with a substrate analogue S, S'-dimethyl FK228 at 1.82 angstrom and 2.00 angstrom, respectively. Structural and biochemical analyses revealed that DepH, in contrast to the well characterized low molecular weight thioredoxin reductases (LMW TrxRs), is an NADP(+)-independent dithiol oxidase. DepH not only lacks a conserved GGGDXAXE motif necessary for NADP(+) binding in the canonical LMW TrxRs, but also contains a 11-residue sequence which physically impedes the binding of NADP(+). These observations explain the difference between NADP(+)-independent small molecule dithiol oxidases and NADP(+)-dependent thioredoxin reductases and provide insights for understanding the catalytic mechanism of dithiol oxidases involved in natural product biosynthesis.
语种: 英语
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/38932
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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作者单位: 中科院上海有机化学研究所

Recommended Citation:
LI JIE,WANG CHENG,ZHANG ZHIMIN,et al. The structural basis of an NADP(+)-independent dithiol oxidase in FK228 biosynthesis[J]. Sci Rep,2014,4:4145.
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