恶性疟原虫脂肪酸生物合成途径中酰基-酰基载体蛋白中间体的主链化学位移归属

Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.

作者信息

Upadhyay Santosh Kumar, Misra Ashish, Surolia Namita, Surolia Avadhesha, Sundd Monica

机构信息

National Institute of Immunology, Aruna Asaf Ali Marg, JNU Campus, New Delhi 110067, India.

出版信息

Biomol NMR Assign. 2010 Apr;4(1):83-5. doi: 10.1007/s12104-010-9212-2. Epub 2010 Feb 25.

DOI:10.1007/s12104-010-9212-2

PMID:20182923

Abstract

We report the backbone chemical shift assignments of the acyl-acyl carrier protein (ACP) intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum. The acyl-ACP intermediates butyryl (C(4)), -octanoyl (C(8)), -decanoyl (C(10)), -dodecanoyl (C(12)) and -tetradecanoyl (C(14))-ACPs display marked changes in backbone HN, C(alpha) and C(beta) chemical shifts as a result of acyl chain insertion into the hydrophobic core. Chemical shift changes cast light on the mechanism of expansion of the acyl carrier protein core.

摘要

我们报告了恶性疟原虫脂肪酸生物合成途径中酰基-酰基载体蛋白（ACP）中间体的主链化学位移归属。由于酰基链插入疏水核心，酰基-ACP中间体丁酰基（C(4)）、辛酰基（C(8)）、癸酰基（C(10)）、十二烷酰基（C(12)）和十四烷酰基（C(14)）-ACP的主链HN、Cα和Cβ化学位移出现显著变化。化学位移变化揭示了酰基载体蛋白核心的扩展机制。