@article {966,
	title = {The mechanism of the reaction catalyzed by ADP-beta-L-glycero-D-manno-heptose 6-epimerase},
	journal = {Journal of the American Chemical Society},
	volume = {126},
	number = {29},
	year = {2004},
	note = {ISI Document Delivery No.: 840JTTimes Cited: 14Cited Reference Count: 24},
	month = {Jul},
	pages = {8878-8879},
	type = {Article},
	keywords = {4, 6-DEHYDRATASE, BACTERIA, D-MANNOHEPTOSE 6-EPIMERASE, EPIMERIZATION, ESCHERICHIA-COLI, GLUCOSE, INSIGHTS, NUCLEOTIDE-MODIFYING ENZYMES, OUTER-MEMBRANE, UDP-GALACTOSE 4-EPIMERASE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000222855300009},
	author = {Read, J. A. and Ahmed, R. A. and Morrison, J. P. and Coleman, W. G. and Tanner, M. E.}
}
@article {4751,
	title = {The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation},
	journal = {Biochemistry},
	volume = {39},
	number = {23},
	year = {2000},
	note = {ISI Document Delivery No.: 324PRTimes Cited: 62Cited Reference Count: 49},
	month = {Jun},
	pages = {7012-7023},
	type = {Article},
	abstract = {Bacterial UDP-glucose dehydrogenase (UDPGlcDH) is essential for formation of the antiphagocytic capsule that protects many virulent bacteria such as Streptococcus pyrogenes and Streptococcus pneumoniae type 3 from the host{\textquoteright}s immune system. We have determined the X-ray structures of both native and Cys260Ser UDPGlcDH from S. pyogenes (74\% similarity to S. pneumoniae) in ternary complexes with UDP-xylose/NAD(+) and UDP-glucuronic acid/NAD(H), respectively. The 402 residue homodimeric UDPGlcDH is composed of an N-terminal NAD(+) dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long (48 Angstrom) central alpha-helix. The first 290 residues of UDPGlcDH share structural homology with 6-phosphogluconate dehydrogenase, including conservation of an active site lysine and asparagine that are implicated in the enzyme mechanism. Also proposed to participate in the catalytic mechanism are a threonine and a glutamate that hydrogen bond to a conserved active site water molecule suitably positioned for general acid/base catalysis.},
	keywords = {alanine, ALIGNMENT, CRYSTAL-STRUCTURE, ESCHERICHIA-COLI, GROUP-A STREPTOCOCCI, INSIGHTS, MECHANISM, MOLECULAR CHARACTERIZATION, REDUCTASE, SUBSTRATE-BINDING},
	isbn = {0006-2960},
	url = {<Go to ISI>://000087631000031},
	author = {Campbell, R. E. and Mosimann, S. C. and van de Rijn, I. and Tanner, M. E. and Strynadka, N. C. J.}
}
