Structural highlights
Function
Q9X1H0_THEMA
Publication Abstract from PubMed
We repurposed the metal-binding site of a cupin superfamily protein into the 2-His-1-carboxylate facial triad, which is one of the common motifs in natural non-heme enzymes, to construct artificial metalloenzymes that can catalyze new-to-nature reactions. The Cu(2+)-H52A/H58E variant catalyzed the stereoselective Michael addition reaction and was found to bear a flexible metal-binding site in the high-resolution crystal structure. Furthermore, the H52A/H58E/F104W mutant accommodated a water molecule, which was supported by Glu58 and Trp104 residues via hydrogen bonding, presumably leading to high stereoselectivity. Thus, the 2-His-1-carboxylate facial triad was confirmed to be a versatile and promising metal-binding motif for abiological and canonical biological reactions.
An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition.,Matsumoto R, Yoshioka S, Yuasa M, Morita Y, Kurisu G, Fujieda N Chem Sci. 2023 Mar 13;14(14):3932-3937. doi: 10.1039/d2sc06809e. eCollection 2023 , Apr 5. PMID:37035687[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsumoto R, Yoshioka S, Yuasa M, Morita Y, Kurisu G, Fujieda N. An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition. Chem Sci. 2023 Mar 13;14(14):3932-3937. PMID:37035687 doi:10.1039/d2sc06809e
