Sigdel, Sujan Singh, Ranjitha Kim, Tae-Su Li, Jinglin Kim, Sang-Yong Kim, In-Won JUNG, WOO SUK Pan, Cheol-Ho Kang, Yun Chan Lee, Jung-Kul 2024-01-20T06:33:39Z 2024-01-20T06:33:39Z 2022-01-25 2015-07 1932-6203 https://pubs.kist.re.kr/handle/201004/125246 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 degrees 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. English PUBLIC LIBRARY SCIENCE Characterization of a Mannose-6-Phosphate Isomerase from Bacillus amyloliquefaciens and Its Application in Fructose-6-Phosphate Production Article 10.1371/journal.pone.0131585 1 PLOS ONE, v.10, no.7 PLOS ONE 10 7 N scie scopus 000358194900018 2-s2.0-84940511374 Multidisciplinary Sciences Science & Technology - Other Topics Article D-FRUCTOSE 6-PHOSPHATE L-ARABINOSE ISOMERASE PHOSPHOMANNOSE ISOMERASE CLONING SUBSTRATE BINDING BIOSYNTHESIS SEQUENCE ENZYMES LACCASE