Publications
Crystal Structures of the histidine acid phosphatase from Francisella tularensis provide insight into substrate recognition. J Mol Biol. 394, 893-904
(2009) Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J Biol Chem. 287, 9041-51
(2012) Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry. 51, 10099-108
(2012) Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol. 10.1016/j.jmb.2018.11.030
(2018) Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens. Proteins. 79, 1215-29
(2011) Crystal structure and tartrate inhibition of Legionella pneumophila histidine acid phosphatase. Arch Biochem Biophys. 585, 32-38
(2015) Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. ACS Chem Biol. 10.1021/acschembio.9b00935
(2020) Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics. Biochemistry. 53, 7794-804
(2014) Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase. Arch Biochem Biophys. 585, 25-31
(2015) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry. 48, 951-9
(2009) Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J. 10.1111/febs.14165
(2017)