Bacterial cellulose pathways

Fructose-1-phospate Figure 10.1 Biochemical pathway for bacterial cellulose. 

Available evidence supports a common ancestry for all cellulose synthases. These enzymes appear to have been a bacterial invention acquired by various eukaryotes via multiple lateral gene transfers. However, the proteins associated with regulation of cellulose biosynthesis and polymer crystallization seem to have evolved independently. Sequence divergence of eukaryotic cellulose synthases and the presence of multiple gene clusters associated with bacterial cellulose synthases are discussed in relation to the possible evolutionary pathways of cellulose biosynthesis. 

Biosynthesis of Bacterial Cellulose 14.2.1 Cellulose Synthesis Metabolic Pathway... 

The biosynthetic pathway that produces bacterial cellulose from glucose and fructose is shown in Fig. 14.2. Glucose is phosphorylated by glucose hexokinase and not by the phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS). The resulting glucose-6-phosphate (G6P) is metabolized through the pentose pathway, because the activity of fructose-6-phosphate (F6P) kinase, which phos-phorylates F6P to fructose-1,6-diphosphate (FDP), is absent in acetic acid bacteria. 

Complement Activation Complement proteins are so-named because they complement antibody activity to eliminate pathogens. The alternate pathway of the complement cascade is normally activated by bacterial surface molecules. Complement activation during dialysis was first identified by the rapid drop in white blood cell counts (neutropenia) during the first 30 min of dialysis. Regenerated cellulose membranes activate complement through the alternate pathway (Chenoweth et al., 1983). Modified cellulose membranes approach the biocompatibility profile of synthetic materials in terms of neutropenia and complement activation. 

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