@article {1279,
	title = {The enzymes of sialic acid biosynthesis},
	journal = {Bioorganic Chemistry},
	volume = {33},
	number = {3},
	year = {2005},
	note = {ISI Document Delivery No.: 931CJTimes Cited: 36Cited Reference Count: 59},
	month = {Jun},
	pages = {216-228},
	type = {Review},
	abstract = {The sialic acids are a family of nine carbon a-keto acids that play a wide variety of biological roles in nature. In mammals, they are found at the distal ends of cell surface glycoconjugates, and thus are major determinants of cellular recognition and adhesion events. In certain strains of pathogenic bacteria, they are found in capsular polysaccharides that mask the organism from the immune system by mimicking the exterior of a mammalian cell. This review outlines recent developments in the understanding of the two main enzymes responsible for the biosynthesis of the sialic acid, N-acetylneuraminic acid. The first, a hydrolyzing UDP-N-acetyl-glucosamine 2-epimerase, generates N-acetylmannosamine and UDP from UDP-N-acetylglucosamine. The second, sialic acid synthase, generates either N-acetylneuraminic acid (bacteria) or N-acetylneuraminic acid 9-phosphate (mammals) in a condensation reaction with phosphoenolpyruvate. An emphasis is placed on an understanding of the mechanistic and structural features of these enzymes. (c) 2005 Elsevier Inc. All rights reserved.},
	keywords = {2-EPIMERASE/N-ACETYLMANNOSAMINE KINASE, BIFUNCTIONAL KEY ENZYME, biosynthesis, ESCHERICHIA-COLI K1, FIRST 2, KDO8P SYNTHASE, MECHANISM, N-ACETYLGLUCOSAMINE 2-EPIMERASE, N-acetylmannosamine, N-ACETYLNEURAMINIC ACID, NEISSERIA-MENINGITIDIS, PHOSPHATE, phosphoenolpyruvate, RAT-LIVER, sialic acid synthase, STEPS, SYNTHASE GENE, UDP-GlcNAc 2-epimerase},
	isbn = {0045-2068},
	url = {<Go to ISI>://000229463100007},
	author = {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.}
}
