Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/21195
Title: Characterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymes
Authors: Li, N
Ma, DL
Liu, X
Wu, L
Chu, X
Wong, KY 
Li, D
Keywords: Congenital erythropoetic porphyria
spiro mechanism
Tetrapyrrole
Urogen III synthase
Uroporphyrinogen III synthase
Issue Date: 2007
Source: Protein journal, 2007, v. 26, no. 8, p. 569-576 How to cite?
Journal: Protein Journal 
Abstract: The structurally related tetrapyrrolic pigments are a group of natural products that participate in many of the fundamental biosynthetic and catabolic processes of living organisms. Urogen III synthase catalyzes a key step in the formation of urogen III, a common intermediate for tetrapyrrolic natural products. In the present study, we cloned, purified, and characterized His-tagged rat urogen III synthase. The mechanism of enzymatic reaction was studied through site-directed mutagenesis of eight highly conserved residues with functional side chains around the active site followed with activity tests. Lys10, Asp17, Glu68, Tyr97, Asn121, Lys147, and His173 have not been studied previously, which were found to be unessential for enzymatic reaction. Tyr168 was identified as an important residue for enzymatic reaction catalyzed by rat urogen III synthase. Molecular modeling suggests the hydroxyl group of Tyr168 side chain is 3.5 Å away from the D ring, and is within hydrogen bond distance (1.9 Å) with acetate side chain of the D ring.
URI: http://hdl.handle.net/10397/21195
ISSN: 1572-3887
DOI: 10.1007/s10930-007-9099-7
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