- Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesisA Hadfield
Department of Biochemistry Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA, 02254 9110, USA
J Mol Biol 289:991-1002. 1999..A histidine residue is identified as a likely acid/base catalyst in the enzymic reaction. Other amino acids implicated in the enzymic activity by mutagenesis are found in the active site region and define the substrate binding pocket...
- Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenaseA Hadfield
Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, England
Biochemistry 40:14475-83. 2001..These results provide a structural explanation for the preferred order of substrate binding that is observed kinetically...
- Critical determinants of host receptor targeting by Neisseria meningitidis and Neisseria gonorrhoeae: identification of Opa adhesiotopes on the N-domain of CD66 moleculesM Virji
Department of Pathology and Microbiology, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK
Mol Microbiol 34:538-51. 1999..These studies define the molecular basis that directs the Opa specificity for the CD66 family and the rationale for tropism of the Opa proteins for the CD66 subgroups...
- Carcinoembryonic antigens are targeted by diverse strains of typable and non-typable Haemophilus influenzaeM Virji
Department of Pathology and Microbiology, and Biochemistry, University of Bristol, Bristol BS8 1TD, UK
Mol Microbiol 36:784-95. 2000....