Biosynthesis of Uridine Diphosphate N-Acetyl-L-Fucosamine in a Cell-Free System from Salmonella arizonae O:59

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T. N. Druzhinina, N. A. Kalinchuk, and V. N. Shibaev^*

Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky pr. 47, 119991 Moscow, Russia; fax: (7-095) 135-5328; E-mail: shiba@ioc.ac.ru

^* To whom correspondence should be addressed.

Received April 15, 2004; Revision received July 7, 2004

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The conversion of uridine diphosphate N-acetyl-D-glucosamine into uridine diphosphate N-acetyl-L-fucosamine was demonstrated with enzymes from cytoplasmic fraction of Salmonella arizonae O:59 cells in the presence of NAD⁺ (NADP⁺) and NADPH. The reaction product was identified by ion-pair, reverse-phase HPLC with the use of synthetic nucleoside diphosphate sugar standards under conditions specially developed for separation of uridine diphosphate 2-acetamido-2,6-dideoxyhexoses. L-Fucose dehydrogenase from porcine liver was shown to be applicable for determination of N-acetyl-L-fucosamine, this enzyme being used to confirm L-configuration of the amino sugar residue in the sugar nucleotide formed.

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KEY WORDS: nucleoside diphosphate sugars, 2-acetamido-2,6-dideoxyhexoses, uridine diphosphate N-acetyl-L-fucosamine, biosynthesis, HPLC, L-fucose dehydrogenase

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