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Literature summary for 1.5.1.7 extracted from

  • Kumar, V.P.; West, A.H.; Cook, P.F.
    Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae (2012), Arch. Biochem. Biophys., 522, 57-61.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
E16Q/C205S the mutation decreases the turnover number by about 15fold Saccharomyces cerevisiae
K13M/C205S the mutation decreases the turnover number by about 15fold Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O Saccharomyces cerevisiae
-
L-lysine + 2-oxoglutarate + NADH
-
r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-NTA column chromatography Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
4°C, His-tagged mutant enzymes in 100 mM HEPES, 300 mM KCl and 300 mM imidazole at pH 8.0, several months, the mutant enzymes maintain stability and remain active Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
N6-(glutaryl-2)-L-lysine: NAD+ oxidoreductase
-
Saccharomyces cerevisiae
SDH
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae