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Literature summary extracted from

  • Ekanayake, D.K.; Andi, B.; Bobyk, K.D.; West, A.H.; Cook, P.F.
    Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts (2010), J. Biol. Chem., 285, 20756-20768.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.7 E122A mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type Saccharomyces cerevisiae
1.5.1.7 E122Q mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type Saccharomyces cerevisiae
1.5.1.7 E78A mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism differs from wild-type, 2-oxoglutarate binds to enzyme and enzyme-NADH Saccharomyces cerevisiae
1.5.1.7 E78A/E122A mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type Saccharomyces cerevisiae
1.5.1.7 E78Q mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type Saccharomyces cerevisiae
1.5.1.7 E78Q/E122Q mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.7 NAD+
-
 Saccharomyces cerevisiae
1.5.1.7 NADH
-
 Saccharomyces cerevisiae
1.5.1.7 oxalylglycine competitive against lysine with mutant E78A, noncompetitive with mutants E78Q, E122Q, E78Q/E122Q, E122A, E78A/E122A Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.7 0.014
-
 NADH mutant E78Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.019
-
 NADH wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.025
-
 NADH mutant E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.036
-
 NADH mutant E78A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.062
-
 NADH mutant E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.11
-
 2-oxoglutarate wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.12
-
 NADH mutant E78Q/E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.133
-
 NADH mutant E78A/E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.18
-
 2-oxoglutarate mutant E78A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.23
-
 2-oxoglutarate mutant E78Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.3
-
 2-oxoglutarate mutant E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.55
-
 2-oxoglutarate mutant E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.62
-
 L-lysine mutant E78A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.9
-
 NAD+ wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 1.1
-
 NAD+ mutant E78Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 1.1
-
 L-lysine wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 2
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine mutant E78Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 2
-
 2-oxoglutarate mutant E78Q/E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 3.3
-
 NAD+ mutant E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 4
-
 L-lysine mutant E78Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 4.8 5 2-oxoglutarate mutant E78A/E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 6.7
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 11
-
 L-lysine mutant E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 14
-
 N6-(L-1,3-dicarboxypropyl)-L-lysine mutant E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 27.1
-
 L-lysine mutant E78Q/E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 36.5
-
 L-lysine mutant E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 190.7
-
 L-lysine mutant E78A/E122A, 25°C, pH 7.2 Saccharomyces cerevisiae

Organism

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

Substrates and Products (Substrate)

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5.1.7 0.015
-
 NADH mutant E78A/E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.017
-
 NADH wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.019
-
 NADH mutant E122A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.038
-
 NADH mutant E78A, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 0.5
-
 NAD+ mutant E78Q, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 1.1
-
 NAD+ wild-type, 25°C, pH 7.2 Saccharomyces cerevisiae
1.5.1.7 1.9
-
 NAD+ mutant E122Q, 25°C, pH 7.2 Saccharomyces cerevisiae