Journal article
Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus
James S Davies, David Coombes, Christopher R Horne, F Grant Pearce, Rosmarie Friemann, Rachel A North, Renwick CJ Dobson
FEBS Letters | WILEY | Published : 2019
Abstract
N-Acetylglucosamine-6-phosphate deacetylase (NagA) and glucosamine-6-phosphate deaminase (NagB) are branch point enzymes that direct amino sugars into different pathways. For Staphylococcus aureus NagA, analytical ultracentrifugation and small-angle X-ray scattering data demonstrate that it is an asymmetric dimer in solution. Initial rate experiments show hysteresis, which may be related to pathway regulation, and kinetic parameters similar to other bacterial isozymes. The enzyme binds two Zn2+ ions and is not substrate inhibited, unlike the Escherichia coli isozyme. S. aureus NagB adopts a novel dimeric structure in solution and shows kinetic parameters comparable to other Gram-positive iso..
View full abstractGrants
Awarded by Marsden Fund Council from Government funding
Awarded by US Army Research Office
Awarded by Ministry of Business, Innovation and Employment Smart Ideas grant
Awarded by Swedish Governmental Agency for Innovation Systems (VINNOVA)
Funding Acknowledgements
RCJD acknowledges the following for funding support, in part: (a) the Marsden Fund Council from Government funding, managed by Royal Society Te Aparangi (contract UOC1506); (b) the US Army Research Laboratory and US Army Research Office (contract W911NF-11-1-0481); (c) a Ministry of Business, Innovation and Employment Smart Ideas grant (contract UOCX1706); and (d) the Biomolecular Interactions Centre (UC). JSD acknowledges the Marsden Fund council from Government funding, managed by Royal Society Te Aparangi (contract UOC1506) for Doctoral Scholarship support. RF acknowledges funding from the Swedish Governmental Agency for Innovation Systems (VINNOVA) (2017-00180) and the Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg. We thank Prof Aron Fenton for helpful feedback on the manuscript.