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Stimulatory factors for enzymatic biotin synthesis from dethiobiotin in cell-free extracts of Escherichia coli.

作者信息

Ohshiro T, Yamamoto M, Bui B T, Florentin D, Marquet A, Izumi Y

机构信息

Department of Biotechnology, Faculty of Engineering, Tottori University, Japan.

出版信息

Biosci Biotechnol Biochem. 1995 May;59(5):943-4. doi: 10.1271/bbb.59.943.

DOI:10.1271/bbb.59.943
PMID:7787312
Abstract

The activity of biotin synthesis from dethiobiotin was found in cell-free extracts of an Escherichia coli bioB transformant. Among the sulfur compounds tested, only S-adenosyl-L-methionine (AdoMet) had a significant effect, while methionine and cysteine were inert. The activity was linearly stimulated by increasing protein concentration. When the dialyzed cell-free extracts were used for the reaction, NADP+, NADPH, and FAD among the well-known cofactors tested promoted the activity. Furthermore, in the presence of AdoMet, cysteine was apparently effective for biotin synthetic activity.

摘要

相似文献

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引用本文的文献

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Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB.生物素合酶中腺苷甲硫氨酸依赖性自由基生成的控制:底物与活性和非活性形式的BioB结合的动力学和热力学分析
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2
Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions.生物素合酶含有两个不同的铁硫簇结合位点:铁硫簇相互转化的化学和光谱电化学分析。
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Biochemistry. 2000 May 2;39(17):5206-14. doi: 10.1021/bi9926227.