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Literature summary extracted from

  • Andi, B.; Xu, H.; Cook, P.F.; West, A.H.
    Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae (2007), Biochemistry, 46, 12512-12521.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.7 expressed in Escherichia coli BL21 (DE3)-RIL cells Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.7 the apo-enzyme is obtained using the hanging drop vapour diffusion method with 100 mM Tris (pH 7.0) and 22% (w/v) PEG 8000, sulfate-, AMP-, and oxalylglycine-bound enzyme crystals are obtained by the hanging drop vapour diffusion method with 26% (w/v) PEG-MME 2000 in 100 mM Tris (pH 7.0) containing 200 mM (NH4)2SO4, or with 24% (w/v) PEG-MME 2000 in 100 mM Bis-Tris, pH 6.5, or with 24% (w/v) PEG-MME 2000 in 100 mM Tris, pH 8.0, at 4°C, respectively Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.7 Saccharomyces cerevisiae P38998
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.7 Ni-NTA column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.7 N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
 Saccharomyces cerevisiae L-lysine + 2-oxoglutarate + NADH
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.5.1.7 N6-(glutaryl-2)-L-lysine:nicotinamide adenine dinucleotide (NAD+) oxidoreductase (L-lysine-forming)
-
 Saccharomyces cerevisiae
1.5.1.7 saccharopine dehydrogenase (L-lysine-forming)
-
 Saccharomyces cerevisiae
1.5.1.7 SDH
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.7 NAD+
-
 Saccharomyces cerevisiae