Article
Crystal structure of LysK, an enzyme catalyzing the last step of lysine biosynthesis in Thermus thermophilus, in complex with lysine: Insight into the mechanism for recognition of the amino-group carrier protein, LysW.
Biochemical and biophysical research communications - 16 Sept 2017
Fujita Satomi, Cho Su-Hee, Yoshida Ayako, Hasebe Fumihito, Tomita Takeo, Kuzuyama Tomohisa, Nishiyama Makoto
Abstract excerpt
LysK is an M20 peptidase family enzyme that hydrolyzes the isopeptide bond between the carrier protein LysW and lysine in order to release lysine, which is the last step of lysine biosynthesis in Thermus thermophilus. In the present study, we determined the crystal structure of LysK in complex with lysine at a resolution of 2.4 Å. The α-amino group of the bound lysine was oriented toward the catalytic center,...
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