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人烟酰胺磷酸核糖转移酶的结晶

Crystallization of human nicotinamide phosphoribosyltransferase.

作者信息

Takahashi Ryo, Nakamura Shota, Yoshida Takuya, Kobayashi Yuji, Ohkubo Tadayasu

机构信息

Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt 5):375-7. doi: 10.1107/S1744309107006069. Epub 2007 Apr 6.

DOI:10.1107/S1744309107006069
PMID:17565174
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2335003/
Abstract

In the NAD biosynthetic pathway, nicotinamide phosphoribosyltransferase (NMPRTase; EC 2.4.2.12) plays an important role in catalyzing the synthesis of nicotinamide mononucleotide from nicotinamide and 5'-phosphoribosyl-1'-pyrophosphate. Because the diffraction pattern of the initially obtained crystals was not suitable for structure analysis, the crystal quality was improved by successive use of the microseeding technique. The resultant crystals diffracted to 2.0 A resolution. These crystals belonged to space group P21, with unit-cell parameters a = 60.56, b = 106.40, c = 82.78 A. Here, the crystallization of human NMPRTase is reported in the free form; the crystals should be useful for inhibitor-soaking experiments on the enzyme.

摘要

在烟酰胺腺嘌呤二核苷酸(NAD)生物合成途径中,烟酰胺磷酸核糖基转移酶(NMPRTase;EC 2.4.2.12)在催化由烟酰胺和5'-磷酸核糖-1'-焦磷酸合成烟酰胺单核苷酸的过程中发挥着重要作用。由于最初获得的晶体的衍射图谱不适用于结构分析,通过连续使用微量接种技术提高了晶体质量。所得晶体的衍射分辨率达到2.0 Å。这些晶体属于空间群P21,晶胞参数为a = 60.56、b = 106.40、c = 82.78 Å。在此,报道了人NMPRTase的游离形式结晶;这些晶体将有助于对该酶进行抑制剂浸泡实验。

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