@article {2510, title = {The Engineering of Bacteria Bearing Azido-Pseudaminic Acid-Modified Flagella}, journal = {Chembiochem}, volume = {10}, number = {8}, year = {2009}, note = {ISI Document Delivery No.: 452SMTimes Cited: 3Cited Reference Count: 24Liu, Feng Aubry, Annie J. Schoenhofen, Ian C. Logan, Susan M. Tanner, Martin E.}, month = {May}, pages = {1317-1320}, type = {Article}, keywords = {4, 6-DEHYDRATASE, azides, biosynthesis, C. jejuni, CAMPYLOBACTER-JEJUNI, cell surfaces, flagella, FUNCTIONAL-CHARACTERIZATION, HELICOBACTER-PYLORI, IDENTIFICATION, METABOLISM, PATHWAY, PROTEINS, PseB, reaction, Staudinger, UDP-N-ACETYLGLUCOSAMINE}, isbn = {1439-4227}, url = {://000266561500009}, author = {Liu, F. and Aubry, A. J. and Schoenhofen, I. C. and Logan, S. M. and Tanner, M. E.} } @article {2193, title = {Mechanistic studies on PseB of pseudaminic acid biosynthesis: A UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase}, journal = {Bioorganic Chemistry}, volume = {36}, number = {4-6}, year = {2008}, note = {ISI Document Delivery No.: 386TPTimes Cited: 2Cited Reference Count: 33Morrison, James P. Schoenhofen, Ian C. Tanner, Martin E.}, month = {Aug-Dec}, pages = {312-320}, type = {Article}, abstract = {UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase (PseB) is a unique sugar nucleotide dehydratase that inverts the C-5 {\textquoteright}{\textquoteright} stereocentre during conversion of UDP-N-acetylglucosamine to UDP-2-acetamido2,6-dideoxy-beta-L-arabino-hexos-4-ulose. PseB catalyzes the first step in the biosynthesis of pseudaminic acid, which is found as a post-translational modification on the flagellin of Campylobacter jejuni and Helicobacter pylori. PseB is proposed to use its tightly bound NADP(+) to oxidize UDP-GlcNAc at C-4 {\textquoteright}{\textquoteright}, enabling dehydration. The alpha,beta unsaturated ketone intermediate is then reduced by delivery of the hydride to C-6 {\textquoteright}{\textquoteright} and a proton to C-5 {\textquoteright}{\textquoteright}. Consistent with this, PseB from C. jejuni has been found to incorporate deuterium into the C-5 {\textquoteright}{\textquoteright} position of product during catalysis in D2O. Likewise, PseB catalyzes solvent isotope exchange into the H-5 {\textquoteright}{\textquoteright} position of product, and eliminates HF from the alternate Substrate, UDP-6-deoxy-6-fluoro-GlcNAc. Mutants of the putative catalytic residues aspartate 126, lysine 127 and tyrosine 135 have severely compromised dehydratase, solvent isotope exchange, and HF elimination activities. (C) 2008 Elsevier Inc. All rights reserved.}, keywords = {6-DEHYDRATASE, Campylobacter jejuni, CAMPYLOBACTER-JEJUNI, dehydratase, DTDP-GLUCOSE 4, ENZYMES, FLAA1, FUNCTIONAL-CHARACTERIZATION, GDP-MANNOSE 4, HELICOBACTER-PYLORI, IDENTIFICATION, Inverting, MOTILITY, PATHWAY, PseB, Pseudaminic acid, UDP-N-acetylglucosamine 5-inverting 4}, isbn = {0045-2068}, url = {://000261905800019}, author = {Morrison, J. P. and Schoenhofen, I. C. and Tanner, M. E.} }