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FEBS Lett. 2018 Nov 9. doi: 10.1002/1873-3468.13289. [Epub ahead of print]

Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus.

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Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg, Sweden.
Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Vic., Australia.


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 isozymes. In summary, these functional data and solution structures are of use for understanding amino sugar metabolism in S. aureus, and will inform the design of inhibitory molecules.


NagA; NagB; amino sugars; analytical ultracentrifugation; enzymology; small-angle X-ray scattering


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