The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH

► A pair of thiols in the vicinity of the dinucleotide-binding site can form a disulfide bond. ► Oxidized enzyme has a higher Kd for NAD+ and a much lower V/Et than wild type enzyme. ► Enzyme exists in two different forms, the disulfide and dithiol forms at low pH. Saccharopine dehydrogenase catalyz...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2011-09, Vol.513 (2), p.71-80
Hauptverfasser:	Bobyk, Kostyantyn D., Kim, Sang Gon, Kumar, Vidya Prasanna, Kim, Sung-Kun, West, Ann H., Cook, Paul F.
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites adenosine monophosphate alpha-ketoglutaric acid Amino Acid Substitution Apoenzymes - chemistry Apoenzymes - genetics Apoenzymes - metabolism apoproteins Base Sequence Catalytic Domain cysteine Cysteine - chemistry deuterium Deuterium Exchange Measurement Disulfide disulfide bonds DNA, Fungal - genetics hydrides Hydrogen-Ion Concentration hydrolysis Isotope effects isotopes Kinetics lysine Lysine - analogs & derivatives Lysine - metabolism Mechanism Models, Molecular Mutagenesis Mutagenesis, Site-Directed mutants mutation NAD - metabolism oxidation Oxidation-Reduction Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RedOx Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Saccharopine dehydrogenase Saccharopine Dehydrogenases - chemistry Saccharopine Dehydrogenases - genetics Saccharopine Dehydrogenases - metabolism solvents Sulfhydryl Compounds - chemistry thiols
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