Journal article
Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae
L Manjunath, SR Guntupalli, MJ Currie, RA North, RCJ Dobson, V Nayak, R Subramanian
Acta Crystallographica Section F Structural Biology Communications | INT UNION CRYSTALLOGRAPHY | Published : 2018
Abstract
Sialic acids are nine-carbon sugars that are found abundantly on the cell surfaces of mammals as glycoprotein or glycolipid complexes. Several Gram-negative and Gram-positive bacteria have the ability to scavenge and catabolize sialic acids to use as a carbon source. This gives them an advantage in colonizing sialic acid-rich environments. The genes of the sialic acid catabolic pathway are generally present as the operon nanAKE. The third gene in the operon encodes the enzyme N-acetylmannosamine-6-phosphate 2-epimerase (NanE), which catalyzes the conversion of N-acetylmannosamine 6-phosphate to N-acetylglucosamine 6-phosphate, thus committing it to enter glycolysis. The NanE enzyme belongs t..
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Awarded by Ministry of Science and Technology
Funding Acknowledgements
This research work was supported by a DBT Indo-Swedish Grant (BT/IN/SWEDEN/41/SR/2013), a DBT B-life grant (BT/PR5081/INF/156/2012) and the NCBS X-ray facility grant (BT/PR12422/MED/31/287/214). We thank the ESRF Access Program of RCB (supported by Grant No. BT/INF/22/SP22660/2017 from the Department of Biotechnology, Ministry of Science and Technology). RD, RN and MC acknowledge the Marsden Fund Council from Government funding, managed by Royal Society Te Aprangi (contract UOC1506).