@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 {2137,
	title = {Synthesis and Enzymatic Incorporation of Modified Deoxyadenosine Triphosphates},
	journal = {European Journal of Organic Chemistry},
	number = {29},
	year = {2008},
	note = {ISI Document Delivery No.: 365YXTimes Cited: 7Cited Reference Count: 35Lam, Curtis Hipolito, Christopher Perrin, David M.},
	month = {Oct},
	pages = {4915-4923},
	type = {Article},
	abstract = {Several deoxyadenosine triphosphates containing modifications at the 8-position have been synthesized. Suitably protected 8-bromodeoxyadenosines were coupled with five imidazole-containing moieties by nucleophilic aromatic substitution or Sonagashira coupling to give modified nucleosides that were then triphosphorylated. Incorporation assays were performed for these modified residues with many commercially available DNA polymerases, and it was found that two of the modified dATPs could be effectively taken up as substrates by Sequenase V2.0. These two residues are candidates for substrates in combinatorial selections in the search for improved catalysis from DNAzymes. ((C) Wiley-VCH Verlag GmbH \& Co. KGaA, 69451 Weinheim, Germany, 2008)},
	keywords = {AMINO-ACID, bioorganic chemistry, CATALYTIC REPERTOIRE, CLEAVING DNA ENZYME, DERIVATIVES, DNA, ENZYMES, FUNCTIONALITIES, HETEROCYCLES, IN-VITRO SELECTION, NUCLEIC-ACIDS, nucleotides, OLIGONUCLEOTIDES, PCR, POLYMERASES, SELEX},
	isbn = {1434-193X},
	url = {<Go to ISI>://000260447200009},
	author = {Lam, C. and Hipolito, C. and Perrin,David M.}
}
@article {335,
	title = {The power distribution advantage of fiber-optic coupled ultraviolet resonance Raman spectroscopy for bioanalytical and biomedical applications},
	journal = {Journal of Raman Spectroscopy},
	volume = {33},
	number = {7},
	year = {2002},
	note = {ISI Document Delivery No.: 580KBTimes Cited: 18Cited Reference Count: 51},
	month = {Jul},
	pages = {503-510},
	type = {Article},
	abstract = {Fiber-optic coupled ultraviolet resonance Raman spectroscopy (FO-UVRRS) of photosensitive biological samples is discussed in the context of both clinical and basic medical research applications. The fiberoptic probes are designed specifically for resonance Raman spectroscopy and offer a power distribution advantage over conventional focusing UVRR spectrometers that allows the use of higher power levels without increasing the risk of photo-damage. A typical fiber-optic probe using a 600 pm core diameter fiber for illumination of the sample allows an increase in power at the sample of over an order of magnitude while maintaining the same power density, and therefore the same level of safety, as a typical conventional UVRR spectrometer. This allows high-quality spectra to be easily obtained in 10 s. Spectra of representative biological samples using high power levels without damage are presented, including the study of a photosensitive enzyme-substrate system under anaerobic conditions. Copyright (C) 2002 John Wiley Sons, Ltd.},
	keywords = {ACTIVATION, AROMATIC-AMINO-ACIDS, BACTERIA, DEEP UV, ENZYMES, LASER EXCITATION, PROBE, SIMPLICITY, SPECTRA, TISSUE},
	isbn = {0377-0486},
	url = {<Go to ISI>://000177232800003},
	author = {Barbosa, C. J. and Vaillancourt, F. H. and Eltis, L. D. and Blades, M. W. and Turner, R. F. B.}
}
@article {335,
	title = {The power distribution advantage of fiber-optic coupled ultraviolet resonance Raman spectroscopy for bioanalytical and biomedical applications},
	journal = {Journal of Raman Spectroscopy},
	volume = {33},
	number = {7},
	year = {2002},
	note = {ISI Document Delivery No.: 580KBTimes Cited: 18Cited Reference Count: 51},
	month = {Jul},
	pages = {503-510},
	type = {Article},
	abstract = {Fiber-optic coupled ultraviolet resonance Raman spectroscopy (FO-UVRRS) of photosensitive biological samples is discussed in the context of both clinical and basic medical research applications. The fiberoptic probes are designed specifically for resonance Raman spectroscopy and offer a power distribution advantage over conventional focusing UVRR spectrometers that allows the use of higher power levels without increasing the risk of photo-damage. A typical fiber-optic probe using a 600 pm core diameter fiber for illumination of the sample allows an increase in power at the sample of over an order of magnitude while maintaining the same power density, and therefore the same level of safety, as a typical conventional UVRR spectrometer. This allows high-quality spectra to be easily obtained in 10 s. Spectra of representative biological samples using high power levels without damage are presented, including the study of a photosensitive enzyme-substrate system under anaerobic conditions. Copyright (C) 2002 John Wiley Sons, Ltd.},
	keywords = {ACTIVATION, AROMATIC-AMINO-ACIDS, BACTERIA, DEEP UV, ENZYMES, LASER EXCITATION, PROBE, SIMPLICITY, SPECTRA, TISSUE},
	isbn = {0377-0486},
	url = {<Go to ISI>://000177232800003},
	author = {Barbosa, C. J. and Vaillancourt, F. H. and Eltis, L. D. and Blades, M. W. and Turner, R. F. B.}
}
@article {4298,
	title = {Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase},
	journal = {Biochemistry},
	volume = {37},
	number = {16},
	year = {1998},
	note = {ISI Document Delivery No.: ZM208Times Cited: 32Cited Reference Count: 35},
	month = {Apr},
	pages = {5746-5754},
	type = {Article},
	abstract = {Studies indicating that the E. coli L-ribulose-5-phosphate 4-epimerase employs an "aldolase-like" mechanism are reported. This NAD(+)-independent enzyme epimerizes a steseocenter that does not bear an acidic proton and therefore it cannot utilize a simple deprotonation-reprotonation mechanism. Sequence similarities between the epimerase and the class II L-fuculose-1-phosphate aldolase suggest that the two may be evolutionarily related and that the epimerization may occur via carbon-carbon bond cleavage and re-formation. Conserved residues thought to provide the metal ion ligands of the epimerase have been modified using site-directed mutagenesis. The resulting mutants show low k(cat) values in addition to a reduced affinity for Zn2+. These observations serve to establish that there is a structural link between between the active site geometry of the epimerase and the aldolase. In addition, the H97N mutant was found to catalyze the condensation of dihydroxyacetone and glycolaldehyde phosphate to produce a mixture of L-ribulose-5-phosphate and D-xylulose-5-phosphate. This observation of aldolase activity establishes that the epimerase active site is capable of promoting carbon-carbon bond cleavage. Furthermore, glycolaldehyde phosphate was shown to be a competitive inhibitor of the mutant enzyme (K-t = 0.37 mM) but not of the wild-type enzyme. The mutation apparently causes the epimerase to become "leaky" and enables it to bind/generate the normal reaction intermediates from the unbound aldol cleavage products.},
	keywords = {ENZYMES, ESCHERICHIA-COLI, L-FUCULOSE-1-PHOSPHATE ALDOLASE, MECHANISM, MUTAGENESIS, ORGANIC-SYNTHESIS, PCR, PURIFICATION, SEQUENCE, SITE},
	isbn = {0006-2960},
	url = {<Go to ISI>://000073515500048},
	author = {Johnson, A. E. and Tanner, M. E.}
}
@article {6413,
	title = {Structural information obtained by negative-ion laser desorption ionization Fourier transform ion cyclotron resonance (l.d.i.-F.t-i.c.r.) mass spectrometry on bacterial capsular polysaccharides},
	journal = {Carbohydrate Research},
	volume = {180},
	number = {2},
	year = {1988},
	note = {ISI Document Delivery No.: V43RVTimes Cited: 5Cited Reference Count: 20Lam, Zamas Dutton, Guy G. S. Comisarow, Melvin B. Weil, David A. Bjarnason, Asgeir},
	month = {Sep},
	pages = {C1-C7},
	type = {Article},
	keywords = {DEGRADATION, DIGOXIN, ENZYMES, GLYCOSIDES, OLIGOSACCHARIDES, SPECTRA},
	isbn = {0008-6215},
	url = {<Go to ISI>://000202953100001},
	author = {Lam, Z. and Dutton, G. G. S. and Comisarow, M. B. and Weil, D. A. and Bjarnason, A.}
}
