Open AccessCrystallization and preliminary X‐ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide
Author(s) -
Youn HyungSeop,
Kim MunKyoung,
Kang Gil Bu,
Kim Tae Gyun,
An Jun Yop,
Lee JungGyu,
Park Kyoung Ryoung,
Lee Youngjin,
Fukuoka ShinIchi,
Eom Soo Hyun
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112040638
Subject(s) - quinolinate , chemistry , phosphoribosyltransferase , crystallization , nad+ kinase , nicotinamide mononucleotide , crystallography , stereochemistry , enzyme , biochemistry , hypoxanthine guanine phosphoribosyltransferase , organic chemistry , tryptophan , amino acid , quinolinic acid , mutant , gene , nicotinamide adenine dinucleotide
Quinolinate phosphoribosyltransferase (QAPRTase) is a key enzyme in NAD biosynthesis; it catalyzes the formation of nicotinate mononucleotide (NAMN) from quinolinate and 5‐phosphoribosyl‐1‐pyrophosphate. In order to elucidate the mechanism of NAMN biosynthesis, crystals of Sus scrofa QAPRTase ( Ss ‐QAPRTase) purified from porcine kidney in complex with NAMN were obtained and diffraction data were collected and processed to 2.1 Å resolution. The Ss ‐QAPRTase–NAMN cocrystals belonged to space group P 321, with unit‐cell parameters a = 119.1, b = 119.1, c = 93.7 Å, γ = 120.0°. The Matthews coefficient and the solvent content were estimated as 3.10 Å 3 Da –1 and 60.3%, respectively, assuming the presence of two molecules in the asymmetric unit.