Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.1.7 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
Search for more literature for 1.5.1.7

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
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
-
 ?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
 Saccharomyces cerevisiae L-lysine + 2-oxoglutarate + NADH + H+
-
 ?

Ki Value [mM]

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