Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus
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 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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Nov 26, 2018
- Source ID
- 10.1002/1873-3468.13289
Entities
People
- Christopher R. Horne
- David Coombes
- F. Grant Pearce
- James S Davies
- Rachel A North
- Renwick Dobson
- Rosmarie Friemann
Organizations
- Ministry of Business, Innovation and Employment
- Swedish Governmental Agency for Innovation Systems
- United States Army Research Laboratory
- University of Canterbury
- University of Gothenburg
- University of Melbourne