通过转移NOESY和饱和转移差异核磁共振研究发现，转羧酶的5S亚基与游离生物素相互作用。
The 5S subunit of transcarboxylase interacts with free biotin as studied by transferred-NOESY and Saturation Transfer Difference NMR.
作者信息
Bhat Rakesh Kumar, Berger Stefan
机构信息
Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, D-04103 Leipzig, Germany.
出版信息
Protein Pept Lett. 2008;15(6):624-9. doi: 10.2174/092986608784966886.
PMID:18680460
Abstract
The 5S subunit of transcarboxylase was expressed and purified. Recent methods of NMR spectroscopy as transferred NOESY, INPHARMA and Saturation Transfer Difference (STD) NMR were used to investigate ligand binding of free biotin to the 5S protein. The binding epitope for biotin is very similar to that obtained at the 12S subunit of transcarboxylase, however no common binding site for pyruvate and biotin exists.
摘要
转羧酶的5S亚基得以表达和纯化。采用了如转移NOESY、INPHARMA和饱和转移差异（STD）核磁共振等最新的核磁共振光谱方法，来研究游离生物素与5S蛋白的配体结合情况。生物素的结合表位与在转羧酶12S亚基上获得的表位非常相似，然而丙酮酸和生物素不存在共同的结合位点。
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