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Literature summary for 1.4.1.3 extracted from

  • Lee, E.Y.; Huh, J.W.; Yang, S.J.; Choi, S.Y.; Cho, S.W.; Choi, H.J.
    Histidine 454 plays an important role in polymerization of human glutamate dehydrogenase (2003), FEBS Lett., 540, 163-166.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
G446D kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis Homo sapiens
H454Y mutation results in depolymerization of hexameric enzyme into active trimers. Mutation has no effect on expression or stability of the protein. The Km-value for NADH is 1.5fold greater than the wild-type value and the KM-value for 2-oxoglutarate is 2.5fold greater than the wild-type value. Vmax values are similar for wild-type and mutant enzyme Homo sapiens
K333L kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis Homo sapiens
K337L kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis Homo sapiens
K344L kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis Homo sapiens
K346L kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis Homo sapiens
S445L kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.076
-
NADH 25°C, mutant enzyme K346L Homo sapiens
0.079
-
NADH 25°C, mutant enzyme K333L Homo sapiens
0.081
-
NADH 25°C, wild-type enzyme Homo sapiens
0.088
-
NADH 25°C, mutant enzyme K337L Homo sapiens
0.089
-
NADH 25°C, mutant enzyme G446D Homo sapiens
0.09
-
NADH 25°C, mutant enzyme K344L Homo sapiens
0.098
-
NADH 25°C, mutant enzyme S445L Homo sapiens
0.122
-
NADH 25°C, mutant enzyme H454Y Homo sapiens
1.25
-
2-oxoglutarate 25°C, wild-type enzyme Homo sapiens
1.29
-
2-oxoglutarate 25°C, mutant enzyme K333L Homo sapiens
1.31
-
2-oxoglutarate 25°C, mutant enzyme K344L Homo sapiens
1.31
-
2-oxoglutarate 25°C, mutant enzyme K346L Homo sapiens
1.45
-
2-oxoglutarate 25°C, mutant enzyme K337L Homo sapiens
1.47
-
2-oxoglutarate 25°C, mutant enzyme S445L Homo sapiens
1.5
-
2-oxoglutarate 25°C, mutant enzyme G446D Homo sapiens
3.13
-
2-oxoglutarate 25°C, mutant enzyme H454Y Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
6 * 56000, mutant enzyme H454Y Homo sapiens
56000
-
6 * 56000, wild-type enzyme and mutant enzymes K333L, K337L, K344L, K346L, S445L and G446L Homo sapiens
160000
-
mutant enzyme H454Y, gel filtration Homo sapiens
330000
-
wild-type enzyme and mutant enzymes K333L, K337L, K344L, K346L, S445L and G446L, gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NADH + NH3
-
Homo sapiens L-glutamate + NAD+ + H2O
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 56000, wild-type enzyme and mutant enzymes K333L, K337L, K344L, K346L, S445L and G446L Homo sapiens
trimer 6 * 56000, mutant enzyme H454Y Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
93
-
NADH 25°C, mutant enzyme K333L Homo sapiens
95
-
NADH 25°C, mutant enzyme H454Y Homo sapiens
98
-
NADH 25°C, mutant enzyme K337L Homo sapiens
100
-
NADH 25°C, mutant enzyme K346L Homo sapiens
102
-
NADH 25°C, mutant enzyme G446D Homo sapiens
104
-
NADH 25°C, wild-type enzyme Homo sapiens
105
-
NADH 25°C, mutant enzyme K344L Homo sapiens
111
-
NADH 25°C, mutant enzyme S445L Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH
-
Homo sapiens