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Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts.
Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.
Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins.
Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae.
Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae.
The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH.
Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB.