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

Journal article
Authors James S Davies
David Coombes
Christopher R Horne
F Grant Pearce
Rosmarie Friemann
Rachel A North
Renwick CJ Dobson
Published in FEBS Letters
Volume 593
Issue 1
Pages 52-66
ISSN 0014-5793
Publication year 2019
Published at Department of Chemistry and Molecular Biology
Centre for antibiotic resistance research, CARe
Pages 52-66
Language en
Links doi.org/10.1002/1873-3468.13289
Keywords sialic acid, antibiotics
Subject categories Biophysics, Biochemistry and Molecular Biology, Structural Biology

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.

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