@article {494,
	title = {Mechanistic aspects of enzymatic carbohydrate epimerization},
	journal = {Natural Product Reports},
	volume = {19},
	number = {3},
	year = {2002},
	note = {ISI Document Delivery No.: 566QLTimes Cited: 21Cited Reference Count: 214},
	month = {Jun},
	pages = {261-277},
	type = {Review},
	abstract = {Carbohydrate epimerases are enzymes that catalyze an inversion of stereochemistry at a stereogenic center in a sugar. This review focuses on the mechanistic strategies that are employed by this diverse family of enzymes, and is divided into the following sections: deprotonation/reprotonation, transient oxidation, cofactor independent, and mutarotation. The review is comprehensive up to Oct. 2001 and contains 216 references.},
	keywords = {2-EPIMERASE, ACETYLNEURAMINIC, ACID BIOSYNTHESIS, D-GLUCOSAMINE 2-EPIMERASE, D-MANNOHEPTOSE 6-EPIMERASE, GDP-L-FUCOSE, GLUCURONYL C-5 EPIMERASE, MANNURONAN C-5-EPIMERASE, N-ACETYLGLUCOSAMINE, RENIN-BINDING PROTEIN, SITE-DIRECTED MUTAGENESIS, UDP-GALACTOSE 4-EPIMERASE, VINELANDII},
	isbn = {0265-0568},
	url = {<Go to ISI>://000176439700001},
	author = {Samuel, J. and Tanner, M. E.}
}
@article {5208,
	title = {Sugar nucleotide-modifying enzymes},
	journal = {Current Organic Chemistry},
	volume = {5},
	number = {2},
	year = {2001},
	note = {ISI Document Delivery No.: 411FKTimes Cited: 12Cited Reference Count: 170},
	month = {Feb},
	pages = {169-192},
	type = {Review},
	abstract = {Sugar nucleotides serve as the activated forms of carbohydrates that are used in a wide range of biosynthetic pathways. Instead of building up the sugar nucleotide from the free sugar itself, nature often chooses to modify the "donor" portion of a pre-existing sugar nucleotide in a biosynthetically efficient manner. In doing so a rich variety of catalytic strategies are employed and this review focuses on recent mechanistic and structural studies of the sugar nucleotide-modifying enzymes. The review is organized around the types of reactions catalyzed and contains the following sections: Epimerases/Mutases/Decarboxylases, Eliminations and Substitutions, Oxidation and Reduction, and Substitutions on the Periphery of Sugar Nucleotides.},
	keywords = {4, 6-DEHYDRATASE, 6-DIDEOXYHEXOSES, ACETYLGLUCOSAMINE 2-EPIMERASE/N-ACETYLMANNOSAMINE, ACETYLNEURAMINIC ACID, biosynthesis, CYTIDINE DIPHOSPHATE 3, D-GLUCOSE, ESCHERICHIA-COLI K-12, FIRST 2, GDP-FUCOSE SYNTHETASE, KINASE, N-ACETYLGLUCOSAMINE, SITE-DIRECTED MUTAGENESIS, STEPS, UDP-GALACTOSE 4-EPIMERASE},
	isbn = {1385-2728},
	url = {<Go to ISI>://000167487300004},
	author = {Tanner, M. E.}
}
@article {4856,
	title = {Binding site analysis of cellulose binding domain CBDN1 from endoglucanse C of Cellulomonas fimi by site-directed mutagenesis},
	journal = {Biochemistry},
	volume = {39},
	number = {30},
	year = {2000},
	note = {ISI Document Delivery No.: 339RJTimes Cited: 17Cited Reference Count: 59},
	month = {Aug},
	pages = {8844-8852},
	type = {Article},
	abstract = {Endoglucanase C (CenC), a beta 1,4 glucanase from the soil bacterium Cellulomonas fimi, binds to amorphous cellulose via two homologous cellulose binding domains, termed CBDN1 and CBDN2. in this work, the contributions of 10 amino acids within the binding cleft of CBDN1 were evaluated by single site-directed mutations to alanine residues. Each isolated domain containing a single mutation was analyzed for binding to an insoluble amorphous preparation of cellulose, phosphoric acid swollen Avicel (PASA), and to a soluble glucopyranoside polymer, barley beta-glucan. The effect of any given mutation on CBD binding was similar for both substrates, suggesting that the mechanism of binding to soluble and insoluble substrates is the same. Tyrosines 19 and 85 were essential for tight binding by CBDN1 as their replacement by alanine results in affinity decrements of approximately 100-fold on PASA, barley beta-glucan, and soluble cellooligosaccharides. The tertiary structures of unbound Y19A and Y85A were assessed by heteronuclear single quantum coherence (HSQC) spectroscopy. These studies indicated that the structures of both mutants were perturbed but that all perturbations are very near to the site of mutation.},
	keywords = {4-GLUCANASE CENC, BETA-1, ESCHERICHIA-COLI, LIGAND-BINDING, LIMITED PROTEOLYSIS, MECHANISM, N-ACETYLGLUCOSAMINE, NUCLEAR-MAGNETIC-RESONANCE, REESEI CELLOBIOHYDROLASE-I, TRICHODERMA-REESEI, TRYPTOPHAN RESIDUES},
	isbn = {0006-2960},
	url = {<Go to ISI>://000088491500018},
	author = {Kormos, J. and Johnson, P. E. and Brun, E. and Tomme, P. and McIntosh, L. P. and Haynes, C. A. and Kilburn, D. G.}
}
