Expression, purification, crystallization and preliminary X-ray analysis of the Met244Ala variant of catalase-peroxidase (KatG) from the haloarchaeon Haloarcula marismortui.

ABSTRACT: The covalent modification of the side chains of Trp95, Tyr218 and Met244 within the active site of Haloarcula marismortui catalase-peroxidase (KatG) appears to be common to all KatGs and has been demonstrated to be particularly significant for its bifunctionality [Smulevich et al. (2006), J. Inorg. Biochem. 100, 568-585; Jakopitsch, Kolarich et al. (2003), FEBS Lett. 552, 135-140; Jakopitsch, Auer et al. (2003), J. Biol. Chem. 278, 20185-20191; Jakopitsch et al. (2004), J. Biol. Chem. 279, 46082-46095; Regelsberger et al. (2001), Biochem. Soc. Trans. 29, 99-105; Ghiladi, Knudsen et al. (2005), J. Biol. Chem. 280, 22651-22663; Ghiladi, Medzihradzky et al. (2005), Biochemistry, 44, 15093-15105]. The Met244Ala variant of the H. marismortui KatG enzyme was expressed in haloarchaeal host cells

SUBMITTER: Ten-I T 

PROVIDER: S-EPMC2339759 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature