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Asian Journal of Biochemistry
Year: 2016  |  Volume: 11  |  Issue: 3  |  Page No.: 118 - 126

Biochemical Leaning of Phosphoglucose Isomerase is More Towards Gluconeogenesis in Pseudomonas aeruginosa PAO1

Arti T. Patel, Rekha C. Akhani, Manisha J. Patel, Samir R. Dedania and Darshan H. Patel    

Abstract: Background: Pseudomonas aeruginosa is an opportunistic and highly versatile in metabolism. Whole genome sequence showed, the organism does not follow the normal glycolysis rather Entner-Doudoroff pathway for energy production. Whole genome sequence annotation shows the presence of glycolytic enzyme. It is important to study biochemical properties of glycolytic enzyme which may reveal the information for its role in other cellular processes. Methodology: Phosphoglucose isomerase, considered as a moonlighting protein by showing the role as an autocrine motility factor, cytokine, neuroleukin, differentiation and maturation factor. Results: The biochemical study revealed that the enzyme is most active under alkaline conditions with optimum pH of 8.0. The higher working temperature is 40°C and it does not require metal ions to initiate isomerization however, metal ion stabilizes the enzyme as compared to apoenzyme. The enzyme showed kcat/Km for glucose 6-phosphate and fructose 6-phosphate is ≈0.078 and ≈1.0 sec–1 mM–1, respectively, which indicates that it has a role in gluconeogenesis rather than glycolysis. Conclusion: Amino acid sequence analysis establishes the evolutionary enzyme by showing conserved active site residues and share ≈48.13% identity with Homo sapiens.

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