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Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus
Author(s) -
Davies James S.,
Coombes David,
Horne Christopher R.,
Pearce F. Grant,
Friemann Rosmarie,
North Rachel A.,
Dobson Renwick C. J.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13289
Subject(s) - amino sugar , biochemistry , staphylococcus aureus , enzyme , chemistry , escherichia coli , isozyme , bacteria , biology , genetics , gene
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 2+ 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.