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

doi:10.1371/journal.pone.0131585

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

Department of Materials Science and Engineering

Research output: Contribution to journal › Article › peer-review

15 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 k_cat/K_m 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 language	English
Article number	e0131585
Journal	PloS one
Volume	10
Issue number	7
DOIs	https://doi.org/10.1371/journal.pone.0131585
Publication status	Published - 2015 Jul 14

ASJC Scopus subject areas

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

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

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.",

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

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AU - Singh, Ranjitha

AU - Kim, Tae Su

AU - Li, Jinglin

AU - Kim, Sang Yong

AU - Kim, In Won

AU - Jung, Woo Suk

AU - Pan, Cheol Ho

AU - Kang, Yun Chan

AU - Lee, Jung Kul

PY - 2015/7/14

Y1 - 2015/7/14

N2 - 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.

AB - 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.

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

Abstract

ASJC Scopus subject areas

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