Dissection of the Stepwise Mechanism to β-Lactam Formation and Elucidation of a Rate-determining Conformational Change in β-Lactam Synthetase

This publication has 67 references indexed in Scilit:

• Rate-Limiting Steps and Role of Active Site Lys443 in the Mechanism of Carbapenam Synthetase
  Biochemistry, 2007
• Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
  Proceedings of the National Academy of Sciences, 2007
• Do Enzymes Change the Nature of Transition States? Mapping the Transition State for General Acid−Base Catalysis of a Serine Protease
  Biochemistry, 2003
• Kinetic Studies on β-Site Amyloid Precursor Protein-cleaving Enzyme (BACE)
  Journal of Biological Chemistry, 2003
• Solvent and Viscosity Effects on the Rate-Limiting Product Release Step of Glucoamylase during Maltose Hydrolysis
  Biotechnology Progress, 1997
• How to measure and predict the molar absorption coefficient of a protein
  Protein Science, 1995
• Slow step after bond-breaking by porcine pepsin identified using solvent deuterium isotope effects
  Biochemical and Biophysical Research Communications, 1991
• Site-directed mutagenesis by overlap extension using the polymerase chain reaction
  Gene, 1989
• Kinetics of Carboxypeptidase Action. I. Effect of Various Extrinsic Factors on Kinetic Parameters¹
  Journal of the American Chemical Society, 1951
• Brownian motion in a field of force and the diffusion model of chemical reactions
  Physica, 1940