ArticlePloS one2015
Characterization of a Mannose-6-Phosphate Isomerase from Bacillus amyloliquefaciens and Its Application in Fructose-6-Phosphate Production.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Functional and genomic evaluation of novel exopolysaccharide produced by marine Pediococcus pentosaceus E3 with antidiabetic, anticancer, and anti-inflammatory potentials.BMC microbiology · 2025Article
- Mannose enhances anti-tumor effect of PLX4032 in anaplastic thyroid cancer.Endocrine-related cancer · 2025Article
- Selective Immobilization of His-Tagged Enzyme on Ni-Chelated Ion Exchange Resin and Its Application in Protein Purification.International journal of molecular sciences · 2023Article
- Identification of Key Gene Networks Controlling Soluble Sugar and Organic Acid Metabolism During Oriental Melon Fruit Development by Integrated Analysis of Metabolic and Transcriptomic Analyses.Frontiers in plant science · 2022Article
- ZIP10 is a negative determinant for anti-tumor effect of mannose in thyroid cancer by activating phosphate mannose isomerase.Journal of experimental & clinical cancer research : CR · 2021Article
- Gastrointestinal Tract and Dietary Fiber Driven Alterations of Gut Microbiota and Metabolites in Durco × Bamei Crossbred Pigs.Frontiers in nutrition · 2021Article
- Phosphate sugar isomerases and their potential for rare sugar bioconversion.Journal of microbiology (Seoul, Korea) · 2020Review
- Microbial and enzymatic strategies for the production of L-ribose.Applied microbiology and biotechnology · 2020Review
- Alternative Substrate Metabolism inFrontiers in microbiology · 2018Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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