High-resolution Structures Reveal Details of Domain Closure and “Half-of-sites-reactivity” in Escherichia coli Aspartate β-Semialdehyde Dehydrogenase

This publication has 19 references indexed in Scilit:

• Capture of an intermediate in the catalytic cycle of l -aspartate-β-semialdehyde dehydrogenase
  Proceedings of the National Academy of Sciences, 2003
• A structural basis for the mechanism of aspartate‐β‐semialdehyde dehydrogenase from Vibrio cholerae
  Protein Science, 2003
• Active Site Analysis of the Potential Antimicrobial Target Aspartate Semialdehyde Dehydrogenase
  Biochemistry, 2001
• The Central Enzymes of the Aspartate Family of Amino Acid Biosynthesis
  Accounts of Chemical Research, 2001
• Structure of Aspartate-β-semialdehyde Dehydrogenase from Escherichia coli, a Key Enzyme in the Aspartate Family of Amino Acid Biosynthesis
  Journal of Molecular Biology, 1999
• The CCP4 suite: programs for protein crystallography
  Acta Crystallographica Section D-Biological Crystallography, 1994
• Chemical and kinetic mechanisms of aspartate-β-semialdehyde dehydrogenase from Escherichia coli
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
• Cloning and characterization of the asd gene of Salmonella typhimurium: use in stable maintenance of recombinant plasmids in Salmonella vaccine strains
  Gene, 1990
• Aspartate‐β‐Semialdehyde Dehydrogenase from Escherichia coli
  European Journal of Biochemistry, 1980
• Chemical reactivity at the catalytic sites of aspartic β-semialdehyde dehydrogenase and glyceraldehyde 3-phosphate dehydrogenase
  Biochemistry, 1973