@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 = {<Go to ISI>://000266561500009},
	author = {Liu, F. and Aubry, A. J. and Schoenhofen, I. C. and Logan, S. M. and Tanner, M. E.}
}
@article {2188,
	title = {Gene expression and metabolism in tomato fruit surface tissues},
	journal = {Plant Physiology},
	volume = {147},
	number = {2},
	year = {2008},
	note = {ISI Document Delivery No.: 308XITimes Cited: 36Cited Reference Count: 115Mintz-Oron, Shira Mandel, Tali Rogachev, Ilana Feldberg, Liron Lotan, Ofra Yativ, Merav Wang, Zhonghua Jetter, Reinhard Venger, Ilya Adato, Avital Aharoni, Asaph},
	month = {Jun},
	pages = {823-851},
	type = {Review},
	abstract = {The cuticle, covering the surface of all primary plant organs, plays important roles in plant development and protection against the biotic and abiotic environment. In contrast to vegetative organs, very little molecular information has been obtained regarding the surfaces of reproductive organs such as fleshy fruit. To broaden our knowledge related to fruit surface, comparative transcriptome and metabolome analyses were carried out on peel and flesh tissues during tomato ( Solanum lycopersicum) fruit development. Out of 574 peel-associated transcripts, 17\% were classified as putatively belonging to metabolic pathways generating cuticular components, such as wax, cutin, and phenylpropanoids. Orthologs of the Arabidopsis ( Arabidopsis thaliana) SHINE2 and MIXTA-LIKE regulatory factors, activating cutin and wax biosynthesis and fruit epidermal cell differentiation, respectively, were also predominantly expressed in the peel. Ultra-performance liquid chromatography coupled to a quadrupole time-of-flight mass spectrometer and gas chromatography-mass spectrometry using a flame ionization detector identified 100 metabolites that are enriched in the peel tissue during development. These included flavonoids, glycoalkaloids, and amyrin-type pentacyclic triterpenoids as well as polar metabolites associated with cuticle and cell wall metabolism and protection against photooxidative stress. Combined results at both transcript and metabolite levels revealed that the formation of cuticular lipids precedes phenylpropanoid and flavonoid biosynthesis. Expression patterns of reporter genes driven by the upstream region of the wax-associated SlCER6 gene indicated progressive activity of this wax biosynthetic gene in both fruit exocarp and endocarp. Peel-associated genes identified in our study, together with comparative analysis of genes enriched in surface tissues of various other plant species, establish a springboard for future investigations of plant surface biology.},
	keywords = {ABC, ARABIDOPSIS-THALIANA, CELL ELONGATION, COTTON FIBER, CUTICULAR STRUCTURE, CUTIN BIOSYNTHESIS, FUNCTIONAL-CHARACTERIZATION, MASS-SPECTROMETRY, MYB TRANSCRIPTION FACTOR, TRANSPIRATION BARRIER PROPERTIES, TRANSPORTER GENE},
	isbn = {0032-0889},
	url = {<Go to ISI>://000256423600034},
	author = {Mintz-Oron, S. and Mandel, T. and Rogachev, I. and Feldberg, L. and Lotan, O. and Yativ, M. and Wang, Z. and Jetter, R. and Venger, I. and Adato, A. and Aharoni, A.}
}
@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 = {<Go to ISI>://000261905800019},
	author = {Morrison, J. P. and Schoenhofen, I. C. and Tanner, M. E.}
}
@article {1464,
	title = {PseG of pseudaminic acid biosynthesis - A UDP-sugar hydrolase as a masked glycosyltransferase},
	journal = {Journal of Biological Chemistry},
	volume = {281},
	number = {30},
	year = {2006},
	note = {ISI Document Delivery No.: 065VFTimes Cited: 12Cited Reference Count: 40Liu, Feng Tanner, Martin E.},
	month = {Jul},
	pages = {20902-20909},
	type = {Article},
	abstract = {The flagellin proteins in pathogenic bacteria such as Campylobacter jejuni and Helicobacter pylori are heavily glycosylated with the nine-carbon alpha-keto acid, pseudaminic acid. The presence of this posttranslational modification is absolutely required for assembly of functional flagella. Since motility is required for colonization, pseudaminic acid biosynthesis represents a virulence factor in these bacteria. Pseudaminic acid is generated from UDP-N-acetylglucosamine in five biosynthetic steps. The final step has been shown to involve the condensation of 2,4-diacetamido- 2,4,6-trideoxy-L-altrose ( 6-deoxy-AltdiNAc) with phosphoenolpyruvate as catalyzed by the enzyme pseudaminic acid synthase, NeuB3. The 6-deoxy-AltdiNAc used in this process is generated from its nucleotide-linked form, UDP-6-deoxy-AltdiNAc, by the action of a hydrolase that cleaves the glycosidic bond and releases UDP. This manuscript describes the first characterization of a UDP-6-deoxy-AltdiNAc hydrolase, namely PseG ( Cj1312) from C. jejuni. The activity of this enzyme is independent of the presence of divalent metal ions, and the values of the catalytic constants were found to be k(cat) = 27 s(-1) and K-m = 174 mu M. The enzyme was shown to hydrolyze the substrate with an overall inversion of stereochemistry at C-1 and to utilize a C-O bond cleavage mechanism during catalysis. These results, coupled with homology comparisons, suggest that the closest ancestors to the hydrolase are members of the metal-independent GT-B family of glycosyltransferases that include the enzyme MurG.},
	keywords = {CAMPYLOBACTER-JEJUNI, FLAGELLIN, FUNCTIONAL-CHARACTERIZATION, GLYCOPROTEINS, glycosylation, HELICOBACTER-PYLORI, IDENTIFICATION, MECHANISM, N-ACETYLGLUCOSAMINE 2-EPIMERASE, NUDIX HYDROLASES, SYNTHASE},
	isbn = {0021-9258},
	url = {<Go to ISI>://000239187300027},
	author = {Liu, F. and Tanner, M. E.}
}
