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TitleFunctional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus.
Journal, issue, pagesFEBS Lett, Vol. 593, Issue 1, Page 52-66, Year 2019
Publish dateNov 26, 2018
AuthorsJames S Davies / David Coombes / Christopher R Horne / F Grant Pearce / Rosmarie Friemann / Rachel A North / Renwick C J Dobson /
PubMed AbstractN-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 ...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 Zn 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.
External linksFEBS Lett / PubMed:30411345
MethodsSAS (X-ray synchrotron)
Structure data

SASDEA6:
Staphylococcus aureus N-acetylglucosamine-6-phosphate deacetylase dimer
Method: SAXS/SANS

SASDEB6:
Staphylococcus aureus glucosamine-6-phosphate deaminase
Method: SAXS/SANS

Source
  • Staphylococcus aureus (strain usa300) (bacteria)
  • Staphylococcus aureus (strain usa300 / tch1516) (bacteria)

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