Abstract
Background:TftG is a YCII superfamily dehydrochlorinase that catalyzes conversion of 5-chlorohydroxyhydroquinone to hydroxybenzoquinone. Results:The TftG crystal structure in complex with product analog 2,5-dihydroxybenzoquinone illustrated the catalytic residues and mechanism. Conclusion:A His-Asp dyad and other conserved signature residues are implicated for catalysis and substrate binding. Significance:This is the first elucidation of a YCII superfamily protein mechanism, which helps explain their obscure nature. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Hayes, R. P., Lewis, K. M., Xun, L., & Kang, C. H. (2013). Catalytic mechanism of 5-chlorohydroxyhydroquinone dehydrochlorinase from the YCII superfamily of largely unknown function. Journal of Biological Chemistry, 288(40), 28447–28456. https://doi.org/10.1074/jbc.M113.499368
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