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FEMS Microbiol Lett. 1999 May 1;174(1):105-9.

Four critical aspartic acid residues potentially involved in the catalytic mechanism of Escherichia coli K-12 WaaR.

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Department of Bacteriology, Nagoya University, School of Medicine, Aichi, Japan.


Escherichia coli K-12 WaaR is a non-processive alpha-1,2 glucosyltransferase, involved in the synthesis of the R-core of lipopolysaccharide. WaaR possesses the four conserved structural regions I, II, III and IV, each presumably involved in the mechanistic function in catalysis. Regions I and III contain the pair of strictly conserved Asp residues. Asp-129, 131 (region I) and 215, 217 (region III) of WaaR were individually converted to Asn by the site-directed mutagenesis of the waaR gene. All mutated enzymes were inactive, supporting the model for an alpha-glycosyl transfer reaction where the pair of strictly conserved aspartic acid residues in regions I and III play a critical role in the catalytic function.

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