Open AccessCrystallization and preliminary crystallographic analysis of N ‐acetyltransferase Mpr1 from Saccharomyces cerevisiae
Author(s) -
Hibi Takao,
Yamamoto Hiromi,
Nakamura Genichi,
Takagi Hiroshi
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109000153
Subject(s) - crystallization , chemistry , saccharomyces cerevisiae , substrate (aquarium) , enzyme , acetylation , oxidative stress , reactive oxygen species , biochemistry , stereochemistry , organic chemistry , biology , yeast , gene , ecology
Mpr1 is an enzyme that catalyzes the N ‐acetylation of the toxic l ‐azetidine‐2‐carboxylic acid (AZC). Recently, Mpr1 has been shown to reduce levels of intracellular reactive oxygen species (ROS) under oxidative stress. The natural substrate involved in the ROS elimination in vivo is still unknown. Mpr1 has been purified and crystallized in space groups P 1 and P 3 1 12. X‐ray data were collected to 1.9 Å resolution from a trigonal crystal soaked with AZC.