Article
The activation mechanism of human porphobilinogen synthase by 2-mercaptoethanol: intrasubunit transfer of a reserve zinc ion and coordination with three cysteines in the active center.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Mar 2005
Sawada Nori, Nagahara Noriyuki, Sakai Tadashi, Nakajima Yoshiaki, Minami Masayasu, Kawada Tomoyuki
Abstract excerpt
Human porphobilinogen synthase [EC.4.2.1.24] is a homo-octamer enzyme. In the active center of each subunit, four cysteines are titrated with 5,5'-dithiobis(2-nitrobenzoic acid). Cys(122), Cys(124) and Cys(132) are placed near two catalytic sites, Lys(199) and Lys(252), and coordinate a zinc ion, referred to as "a proximal zinc ion", and Cys(223) is placed at the orifice of the catalytic cavity and coordinates a...
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