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Literature summary for 1.5.1.7 extracted from

  • Bobyk, K.D.; Kim, S.G.; Kumar, V.P.; Kim, S.K.; West, A.H.; Cook, P.F.
    The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH (2011), Arch. Biochem. Biophys., 513, 71-80.
    View publication on PubMed
Search for more literature for 1.5.1.7

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
C205S the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by more than 30fold for the C205S mutant Saccharomyces cerevisiae
C205V the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by 5fold for the C205V mutant Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 NADH mutant enzyme C205S, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.019
-
 NADH wild type enzyme, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.05
-
 NADH mutant enzyme C205V, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.11
-
 2-oxoglutarate wild type enzyme, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.11
-
 2-oxoglutarate mutant enzyme C205S, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.2
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine mutant enzyme C205S, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.38
-
 2-oxoglutarate mutant enzyme C205V, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.89
-
 L-lysine mutant enzyme C205S, at pH 7.0 and 25°C Saccharomyces cerevisiae
0.9
-
 NAD+ wild type enzyme, at pH 7.0 and 25°C Saccharomyces cerevisiae
1.1
-
 L-lysine wild type enzyme, at pH 7.0 and 25°C Saccharomyces cerevisiae
1.2
-
 NAD+ mutant enzyme C205V, at pH 7.0 and 25°C Saccharomyces cerevisiae
1.4
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine mutant enzyme C205V, at pH 7.0 and 25°C Saccharomyces cerevisiae
1.8
-
 NAD+ mutant enzyme C205S, at pH 7.0 and 25°C Saccharomyces cerevisiae
3
-
 L-lysine mutant enzyme C205V, at pH 7.0 and 25°C Saccharomyces cerevisiae
6.7
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine wild type enzyme, at pH 7.0 and 25°C Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41464
-
 x * 41464, calculated from amino acid sequence Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni–NTA affinity column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 41464, calculated from amino acid sequence Saccharomyces cerevisiae

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1
-
 NAD+ wild type enzyme, at pH 7.0 and 25°C Saccharomyces cerevisiae
1.4
-
 NAD+ mutant enzyme C205S, at pH 7.0 and 25°C Saccharomyces cerevisiae
1.5
-
 NAD+ mutant enzyme C205V, at pH 7.0 and 25°C Saccharomyces cerevisiae