Structural Studies of the Final Enzyme in the α-Aminoadipate Pathway-Saccharopine Dehydrogenase from Saccharomyces cerevisiae

The 1.64 Å structure of the apoenzyme form of saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae shows the enzyme to be composed of two domains with similar dinucleotide binding folds with a deep cleft at the interface. The structure reveals homology to alanine dehydrogense, despite low...

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Veröffentlicht in:	Journal of molecular biology 2007-10, Vol.373 (3), p.745-754
Hauptverfasser:	Burk, D.L., Hwang, J., Kwok, E., Marrone, L., Goodfellow, V., Dmitrienko, G.I., Berghuis, A.M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine Dehydrogenase - chemistry Alanine Dehydrogenase - metabolism ALANINES Amino Acid Sequence antifungals Binding Sites CATALYSIS CONFORMATIONAL CHANGES CRYSTAL STRUCTURE Crystallography, X-Ray drug design enzyme mechanism ENZYMES FUNGI Lysine - analogs & derivatives Lysine - metabolism lysine biosynthesis MATERIALS SCIENCE Models, Molecular Molecular Sequence Data NAD - metabolism national synchrotron light source OXIDOREDUCTASES Protein Conformation proton shuttle PROTONS RESIDUES SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - growth & development Saccharopine Dehydrogenases - chemistry Saccharopine Dehydrogenases - isolation & purification Saccharopine Dehydrogenases - metabolism Sequence Homology, Amino Acid SUBSTRATES TARGETS
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