Characterization of a Mannose-6-Phosphate Isomerase from Bacillus amyloliquefaciens and Its Application in Fructose-6-Phosphate Production

Sujan Sigdel, Ranjitha Singh, Tae Su Kim, Jinglin Li, Sang Yong Kim, In Won Kim, Woo Suk Jung, Cheol Ho Pan, Yun Chan Kang, Jung Kul Lee

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The BaM6PI gene encoding a mannose-6-phosphate isomerase (M6PI, EC 5.3.1.8) was cloned from Bacillus amyloliquefaciens DSM7 and overexpressed in Escherichia coli. The enzyme activity of BaM6PI was optimal at pH and temperature of 7.5 and 70°C, respectively, with a kcat/Km of 13,900 s-1 mM-1 for mannose-6-phosphate (M6P). The purified BaM6PI demonstrated the highest catalytic efficiency of all characterized M6PIs. Although M6PIs have been characterized from several other sources, BaM6PI is distinguished from other M6PIs by its wide pH range and high catalytic efficiency for M6P. The binding orientation of the substrate M6P in the active site of BaM6PI shed light on the molecular basis of its unusually high activity. BaM6PI showed 97% substrate conversion from M6P to fructose-6- phosphate demonstrating the potential for using BaM6PI in industrial applications.

Original languageEnglish
Article numbere0131585
JournalPloS one
Volume10
Issue number7
DOIs
Publication statusPublished - 2015 Jul 14

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Sigdel, S., Singh, R., Kim, T. S., Li, J., Kim, S. Y., Kim, I. W., Jung, W. S., Pan, C. H., Kang, Y. C., & Lee, J. K. (2015). Characterization of a Mannose-6-Phosphate Isomerase from Bacillus amyloliquefaciens and Its Application in Fructose-6-Phosphate Production. PloS one, 10(7), [e0131585]. https://doi.org/10.1371/journal.pone.0131585