A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenaseKeith Hart, J. John Holbrook, Tony Atkinson et al.|Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|1987Cited by 67
The use of a genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzymeAdam Waldman, J. John Holbrook, Keith Hart et al.|Biochemical and Biophysical Research Communications|1988Cited by 66
The use of site-directed mutagenesis and time-resolved fluorescence spectroscopy to assign the fluorescence contributions of individual tryptophan residues in Bacillus stearothermophilus lactate dehydrogenaseAdam Waldman, J. John Holbrook, Ian Munro et al.|Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|1987Cited by 23