Open AccessCrystallization of human nicotinamide phosphoribosyltransferase
Author(s) -
Yoshida Takuya,
Nakamura Shota,
Takahashi Ryo,
Kobayashi Yuji,
Ohkubo Tadayasu
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107006069
Subject(s) - nicotinamide phosphoribosyltransferase , crystallization , phosphoribosyltransferase , chemistry , materials science , biochemistry , hypoxanthine guanine phosphoribosyltransferase , nad+ kinase , organic chemistry , enzyme , mutant , gene
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 initally 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 Å resolution. These crystals belonged to space group P 21, with unit‐cell parameters a = 60.56, b = 106.40, c = 82.78 Å. Here, the crystallization of human NMPRTase is reported in the free form; the crystals should be useful for inhibitor‐soaking experiments on the enzyme.