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J Biol Chem, Vol. 274, Issue 1, 424-429, January 1, 1999

Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis

Toshiyuki Mio, Toshiko Yamada-Okabe^§, Mikio Arisawa, and Hisafumi Yamada-Okabe

From the  Department of Mycology, Nippon Roche Research Center, 200 Kajiwara, Kamakura, Kanagawa 247-8530 and the ^§ Department of Hygiene, School of Medicine, Yokohama City University, 3-9 Fukuura, Kanazawa, Yokohama 236-0004, Japan

The Saccharomyces cerevisiae gene, YFL017C, for a putative acetyltransferase was characterized. Disruption of YFL017C was lethal, leading to a morphology similar to those caused by the depletion of AGM1 or UAP1, the genes encoding phospho-N-acetylglucosamine mutase and UDP-N-acetylglucosamine pyrophosphorylase, respectively. This implies the involvement of YFL017C in UDP-N-acetylglucosamine synthesis. The recombinant protein for YFL017C displayed phosphoglucosamine acetyltransferase activities in vitro and utilized glucosamine 6-phosphate as the substrate. When incubated with Agm1p and Uap1p, the Yfl017c protein produced UDP-N-acetylglucosamine from glucosamine 6-phosphate. These results indicate that YFL017C specifies glucosamine-6-phosphate acetyltransferase; therefore, the gene was designated GNA1 (glucosamine-6-phosphate acetyltransferase). In addition, whereas bacterial phosphoglucosamine acetyltransferase and UDP-N-acetylglucosamine pyrophosphorylase activities are intrinsic in a single polypeptide, they are encoded by distinct essential genes in yeast. When the sequence of ScGna1p was compared with those of other acetyltransferases, Ile⁹⁷, Glu⁹⁸, Val¹⁰², Gly¹¹², Leu¹¹⁵, Ile¹¹⁶, Phe¹⁴², Tyr¹⁴³, and Gly¹⁴⁷ were found to be highly conserved. When alanine was substituted for these amino acids, the enzyme activity for the substituted Phe¹⁴² or Tyr¹⁴³ enzymes was severely diminished. Although the activity of Y143A was too low to perform kinetics, F142A displayed a significantly increased K_m value for acetyl-CoA, suggesting that the Phe¹⁴² and Tyr¹⁴³ residues are essential for the catalysis.

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