Detail Information
Publications
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....
