This reveals that mutant cells do not die in the presence of GlcNAc and only their growth has been inhibited. Atomic force microscopy was employed to analyze cell morphology and no significant changes were observed between wild type and mutant cells. In the present study, we report a genomic DNA fragment belonging to N-acetylglucosamine 6-phosphate deacetylase from cellulose producing bacterium G. xylinus. In E. coli and other prokaryotes, nagA is demonstrated to be involved in GlcNAc metabolisms by deacetylating GlcNAc-6-P to Gln-6-P. Therefore we sought to investigate the role of nagA in N-acetylglucosamine assimilation in G. xylinus by disrupting nagA. Since nagA mutants were able to grow on glucosamine, this clearly indicates that deacetylase is not involved in glucosamine degradation. Due to the fact that UDP-GlcNAc was almost undetectable in DnagA cells under either glucose or GlcNAc feed, we not only conclude that nagA is essential for conversion of GlcNAc supplements in to UDP-GlcNAc but also that G. xylinus lacks the enzyme AGM, as in presence AGM bacteria would be able to synthesize UDP-GlcNAc even in the absence of nagA. Based on our results and the GlcNAc metabolic pathway from both prokaryotes and eukaryotes, we believed that following steps occurred in G. xylinus: i) conversion of GlcNAc-6-phosphate into glucosamine-6-phosphate by NagA; ii) conversion of GlcN-6-P into glucosamine-1-phosphate ; iii) acetylation of GlcN-1-P to produce N-acetylglucosamine-1-phosphate ; and iv) synthesis of UDP-GlcNAc from GlcNAc-1- P and UTP. The overall pathway is illustrated in Fig. 6. The growth characteristics of deacetylaseless mutants confirm the catabolic routes for glucosamine and GlcNAc in G. xylinus. The inhibited growth of mutants in presence of GlcNAc was due to lack of adequate UDP-GlcNAc in cytoplasm for peptidoglycan cell wall synthesis; as a result the bacteria could not multiply. Earlier studies have shown that G. xylinus is able to incorporate GlcNAc in cellulose while grown under GlcNAc fed conditions. Therefore we sought to evaluate the chemical composition of cellulose produced by both wild type and mutant cells and the role of nagA in this procedure. We did not observe any GlcNAc content in cellulose produced by mutant cells while a small fraction of GlcNAc was observed in wild type cells as reported earlier.