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Literature summary 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)

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

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Storage Stability

EC Number Storage Stability Organism
1.5.1.7 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)

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: NAD+ oxidoreductase
-
Saccharomyces cerevisiae
1.5.1.7 SDH
-
Saccharomyces cerevisiae

Cofactor

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