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2-aminobutyrate + H2O + NADP+
2-oxobutyrate + NH3 + NADPH
-
3% of activity with L-glutamate
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
homocysteinesulfinate + H2O + NAD(P)+
?
-
-
-
-
?
L-glutamate + H2O + 2-azido-NAD+
2-oxoglutarate + NH3 + 2-azido-NADH
-
-
-
?
L-glutamate + H2O + N6-(2-aminoethyl)-NAD(P)+
2-oxoglutarate + NH3 + N6-(2-aminoethyl)-NAD(P)H
-
-
-
?
L-glutamate + H2O + N6-(2-aminoethyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-aminoethyl)-NADH + H+
-
-
-
-
r
L-glutamate + H2O + N6-(2-hydroxy-2-trimethylammoniumpropyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-hydroxy-2-trimethylammoniumpropyl)-NADH + H+
-
-
-
-
r
L-glutamate + H2O + N6-(2-hydroxy-3-trimethylammoniumpropyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-hydroxy-3-trimethylammoniumpropyl)-NADH
-
-
-
?
L-glutamate + H2O + N6-(3-sulfonatopropyl)-NAD+
2-oxoglutarate + NH3 + N6-(2-sulfonatopropyl)-NADH
-
-
-
?
L-glutamate + H2O + N6-poly(ethyleneglycol)-N6-(2-aminoethyl)-NAD+
2-oxoglutarate + NH3 + )poly(ethyleneglycol)-N6-(2-aminoethyl)-NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + poly(ethyleneglycol)-N6-(2-aminoethyl)-NADP+
2-oxoglutarate + NH3 + poly(ethyleneglycol)-N6-(2-aminoethyl)-NADPH + H+
-
-
-
-
r
L-glutamate + H2O + polyethylenglycol-N6-(2-aminoethyl)-NAD(P)+
2-oxoglutarate + NH3 + polyethylenglycol-N6-(2-aminoethyl)-NAD(P)H
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
norvaline + H2O + NAD(P)+
2-oxopentanoate + NH3 + NAD(P)H
-
-
-
-
?
norvaline + H2O + NADP+
2-oxovalerate + NH3 + NADPH
-
activity is 20% of that observed in the presence of 2-oxoglutarate and L-glutamate
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
valine + H2O + NADP+
2-oxovalerate + NH3 + NADPH
-
3% of activity with L-glutamate
-
?
additional information
?
-
2-oxoglutarate + NAD(P)H + NH3

L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3

L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
no activity with NAD+ as cofactor
-
-
ir
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3

L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NH3 + NADH

L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
?
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
specific activity in the presence of NADH is about 30% of that with NADPH
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+

L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADPH + H+

L-glutamate + H2O + NADP+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
?
alanine + H2O + NAD(P)+

pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
-
very low activity
-
-
?
L-glutamate + H2O + NAD(P)+

2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
highly specific for 2-oxoglutarate and glutamate
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
enzyme for the main route for ammonia assimilation at low concentrations of ammonia
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
very low activity with: leucine, alpha-aminobutyrate, valine, isoleucine and methionine
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
rate of glutamate synthesis is several-fold higher than the rate for the reverse reaction
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
dogfish
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
highly specific for 2-oxoglutarate and glutamate
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+

2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD+

2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
ir
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+

2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
ir
L-glutamate + NAD+ + H2O

2-oxoglutarate + NADH + NH3
-
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
r
additional information

?
-
-
the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH
-
-
?
additional information
?
-
-
the glutamate formation activity is 3fold higher than the glutamate deamination activity
-
-
?
additional information
?
-
-
no activity in the amination reaction direction with NADH or NADPH, 2-oxoglutarate and ammonia
-
-
?
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2-Azido-NAD+
-
0.1 mM, 60% inhibition after 3 min of photolabeling
4-iodoacetamidosalicylic acid
-
-
8-azidoguanosine 5'-triphosphate
-
used for affinity photolabeling, 0.1 mM, 95% inhibition
alanine
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
AlCl3
-
increase in sensitivity to aluminium as pH decreases, inhibitory effect is predominant below pH 7.0, no effect above pH 8.5. Completely inactivated enzyme contains 2 mol of aluminum per mol of subunit. Citrate, NaF, N-(2-hydroxyethyl) ethylenediaminetriacetic acid or EDTA efficiently protects against inactivation. Citrate and NaF release aluminum from the completely inactivated aluminum-enzyme complex and fully recover enzyme activity. Binding of aluminum induces a decrease in alpha helices and beta sheets and an increase in random coil
alpha-Ketoglutarate oxime
-
-
alpha-Monofluoroglutarate
-
-
Aminooxyacetate
-
5 mM, weak inhibition of isozymes 1-3
AMP
-
inhibits only NADPH-linked activity
Chloroquine
-
potent inhibitor of isozymes GDH1 and GDH2 at a dose-dependent manner, the inhibitory effect of chloroquine on GDH2 is abolished by the presence of ADP and L-leucine, whereas GTP does not change the sensitivity to chloroquine inhibition, shows a non-competitive inhibition against 2-oxoglutarate and an uncompetitive inhibition against NADH
citrate
-
10 mM, 60% inhibition of oxidative deamination
GDP
strong allosteric inhibitor of GDH1 leading to a 90% reduction of activity. Addition of increasing concentrations of pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm) leads to an increasing protection from GDP inhibition
histidine
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
KCN
-
50 mM, strong inhibition of isozymes 1-3
L-aspartate
-
inhibition of NADPH linked reaction, activation of NAD(H) linked reaction
lysine
-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
malate
-
5 mM, complete inhibition of NADH-linked activity
Methylacetimidate
-
100 mM, moderate inhibition of isozymes 1-3
methylglyoxal
with 1 mM methylglyoxal, GDH activity significantly decreases at 30 min of incubation, and markedly drops by 37% within 5 h compared to control
N-(N'-acetyl-4-sulfamoylphenyl)maleimide
-
-
NADH
-
high concentration
Ni2+
-
1 mM, moderate inhibition of isozymes 1-3
o-phenanthroline
-
5 mM, strong inhibition of isozymes 1-3
o-phthalaldehyde
-
0.1 mM, 98% inhibition after 5 min at 60°C, competitive vs. 2-oxoglutarate and NADH
oxalylglycine
-
competitive vs. 2-oxoglutarate, uncompetitive vs. NADPH, noncompetitive vs. NH4+
p-chloromercuribenzoic acid
-
progressive decrease in enzyme activity of both isoenzymes, inhibition is not affected by addition of GTP or ADP
p-hydroxymercuribenzoate
-
5 mM, moderate inhibition of isozymes 1-3
Phenylglyoxal
-
4 mM, 75% inhibition, uncompetitive vs. 2-oxoglutarate, noncompetitive vs. NADH
phosphate
-
pH 8.0-9.0: activation, pH 6.0-7.6: almost complete inhibition with 400 mM
phosphatidylserine
-
assumed to be a simple non-competitive inhibition
pyridoxal
-
NADH and NADPH protect from inactivation
Sodium acetate
-
at 5°C only
sodium dodecylsulfate
-
time-dependent irreversible inhibition, 0.2 mM, 37% inhibition, 0.15 mM, 50% inhibition after 30 min, in the presence of 2-oxoglutarate after 370 min
succinate
-
5 mM, complete inhibition of NADH-linked activity
Zn2+
-
1 mM, strong inhibition of isozymes 1-3
2-oxoglutarate

-
-
ADP

-
-
ADP
-
above pH 7.0: allosteric activation, pH 6.0-7.0: strong inhibition
ATP

-
-
ATP
-
strong inhibition at 37°C, no inhibition at 5°C
ATP
-
wild-type: inhibition at 0.1 mM and between 0.5-1.0 mM and above, activation at 1 mM, H454Y and S448P mutant enzyme: activation between 0.1-1 mM, inhibition above, R463A mutant enzyme: progressive inhibition between 0.01 and 10 mM
ATP
-
1 mM, 65% inhibition of NADH reaction due to chelating properties of ATP
ATP
-
membrane-bound enzyme form, inhibition of microtubule-binding activity
ATP
-
strong inhibition at 37°C, no inhibition at 5°C
D-glutamate

-
10 mM, 57% inhibition of NADP+-linked activity, 30% inhibition of NADPH-linked activity
D-glutamate
-
2 mM, 11% inhibition, 6 mM, 34% inhibition
diethylstilbestrol

-
-
EDTA

-
5 mM, 80-90% inhibition of isozymes 1-3
EDTA
-
complete loss of NADH and NAD+ activities, NADPH activity unaffected
fumarate

-
-
glutamate

-
weak inhibition at pH 8.5, strong inhibition at pH 10.0
Glutarate

-
-
Glutarate
-
shows no affinity for N6-linked NAD+ but is biospecifically adsorbed to S6-linked NAD+ derivatives in the presence of its soluble kinetic-based enzyme capture ligand glutarate
Glyoxal

-
-
Glyoxal
67% inhibition at 1 mM
GTP

-
-
GTP
-
inhibition at pH 9.0, activation in presence of electrolytes at pH 6.0
GTP
-
0.06 mM, 95% inhibition
GTP
-
GTP inhibition is attenuated to some extent by the proteolysis with TLCK-treated chymotrypsin
GTP
-
allosteric regulation, low inhibition of the deamination reaction and strong inhibition of the amination reaction
GTP
-
little inhibition of H454Y mutant enzyme
GTP
inhibition of wild-type enzyme and mutant enzymes r470H and N498S. No inhibition of mutant enzyme G456A. IC50 of wild-type enzyme is 0.00019 mM, IC50 of mutant enzyme G456A is 0.0028 mM, IC50 of mutant enzyme R470G is 0.00017 mM, IC50 of mutant enzyme N498S is 0.0002 mM
GTP
-
inhibits wild-type enzyme and mutant enzyme E279G
GTP
-
IC50 for wild-type GLUD1: 0.0122 mM, IC50 for mutant enzyme R443S: 0.0162 mM, IC50 for mutant enzyme M415L: 0.0147 mM, IC50 for mutant enzyme M370L: 0.0113 mM, IC50 for mutant enzyme S331T: 0.0108 mM
GTP
potent inhibitor. IC50 for wild-type enzyme is 0.00019 mM, IC50 for mutant enzyme G456A is 0.0028 mM. ADP renders the GLUD1-derived enzyme less sensitive to GTP inhibition; totally insensitive to, it becomes amenable to GTP inhibition in presence of ADP
GTP
-
inhibits isozyme GDH1
GTP
-
efective inhibitor: activity below 10% of its full activity; GDH2 is resistent to GTP inhibition
GTP
negative allosteric regulator
GTP
-
1 mM, 42% inhibition due to chelating properties of GTP
GTP
8.23% activity in the presence of 0.01 mM ATP
GTP
-
membrane-bound liver enzyme, complete inhibition
GTP
-
allosteric regulation, low inhibition of the deamination reaction and strong inhibition of the amination reaction
GTP
-
strong inhibition at 37°C, weak inhibition at 5°C
isophthalate

-
-
isophthalate
-
competitive vs. glutamate
NaCl

-
100 mM, 50% inhibition of NADH and NAD+ dependent reactions
NAD+

-
incubation with 0.1 mM for 60 min inhibits hGDH1 and hGDH2 by 75% and 70%, respectively, incubations for longer time periods up to 3 h, does not further increase the inhibition of hGDH isoenzymes, ADP-ribosylated hDGH isozymes are reactivated by Mg2+-dependent mitochondrial ADP-ribosylcysteine hydrolase
oxaloacetate

-
5 mM, 79% inhibition of oxidative deamination
oxaloacetate
-
5 mM, 20-25% inhibition of NADH- and NAD+-dependent activities
palmitoyl-CoA

-
-
palmitoyl-CoA
-
concentration-dependent inhibition, GDH1 is less sensitive to palmitoyl-CoA inhibition than GDH2
pyridoxal 5'-phosphate

-
5 mM, 100% inhibition
pyridoxal 5'-phosphate
dogfish
-
NAD+ and NADP+ protect from inactivation in the presence of sodium glutarate
pyridoxal 5'-phosphate
-
2 mM, complete loss of activity
pyridoxal 5'-phosphate
-
0.11 mM, approx. 30% inactivation after 10 min, 0.78 mM, 80% inactivation, inactivation is completely reversed by dialysis
additional information

-
complex inhibition pattern for ATP, GTP, NaCl, KCl, sodium acetate, NaI, and potassium nitrate of forward and reverse reaction at 5°C and 37°C
-
additional information
-
GDH2 is resistant to GTP inhibition
-
additional information
-
no inhibition or activation in the presence of ADP, GTP and leucine
-
additional information
-
complex inhibition pattern for ATP, GTP, NaCl, KCl, sodium acetate, NaI, and potassium nitrate of forward and reverse reaction at 5°C and 37°C
-
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2-mercaptoethanol
-
2fold activation
8-azidoguanosine 5'-diphosphate
-
used for affinity photolabeling
chymotrypsin
-
0.2 mg/ml chymotrypsin cleaves glutamate dehydrogenase in such a fashion as to cause a rise in activity with NADP+ and NAD+ as coenzyme, over threefold activation in the NADP+ assay with TLCK-treated chymotrypsin, the distinguishing aspect with untreated chymotrypsin is that the activation is followed by a decrease in activity
-
glutathione
-
2fold activation
KCl
-
activates at 5°C and 37°C
L-aspartate
-
2fold activation of glutamate synthesis
L-His
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
N6-(2-aminoethyl)-NAD+
-
-
N6-(2-aminoethyl)-NADP+
-
-
N6-(2-Hydroxy-3-trimethylammonium propyl)-NAD+
-
-
N6-(3-sulfonatopropyl)-NAD+
-
-
NaCl
-
activates at 37°C only
phosphate
-
activator at pH 8.0-9.0, inhibitor at pH 6.0-7.6
PMP-BCATm
pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm) accelerates the oxidative deamination reaction of GDH1in the presence of branched-chain amino acids (Leu, Ile, Val). Reductive amination reaction is not affected
-
Poly(ethylene glycol)-N6-(2-aminoethyl)-NAD+
-
-
-
Poly(ethylene glycol)-N6-(2-aminoethyl)-NADP+
-
-
-
Trypsin
-
limited trypsin proteolyis activates the purified enzyme 8fold if the peptide is absent from the assay mixture, the native enzyme is 3fold activated if the cleaved peptide is present, activation may therefore be induced by loss of the peptide from the subunit of the native enzyme
-
ADP

-
-
ADP
-
above pH 7.0: allosteric activation
ADP
-
pH 6.0-7.0: strong inhibition
ADP
-
activation only if concentrations of both NAD(P)+ and substrate are high
ADP
-
1.5fold activation, 0.08 mM NADH as cofactor
ADP
-
increases the activity up to 2.3fold
ADP
-
ADP activation is almost abolished after treatment with TLCK-treated chymotrypsin
ADP
-
allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 1100% activation by ADP. Relative activation by ADP of GDH-catalyzed NAD+reduction is 36%, compared with 198% for NADP+ reduction
ADP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
ADP
-
no activation of R463A mutant enzyme
ADP
-
0.1-1.0 mM, activates wild-type enzyme and mutant enzyme E279G
ADP
-
1 mM, pH 8.0, 3fold activation of wild-type enzyme, no significant actication of Tyr187 mutant enzymes
ADP
in absence of GTP the isoenzyme GLUD2 assumes a conformational state associated with little catalytic activity, it remains amenable to full activation by ADP and/or L-Leu
ADP
-
ADP displays a lower affinity for hGDH2 than for hGDH1
ADP
positive allosteric regulator
ADP
the addition of FLAG tag to the C-terminus of GDH leaves the recombinant protein fivefold less sensitive to ADP activation
ADP
120.88% activity in the presence of 0.25 mM ATP
ADP
ADP induces an allosteric conformational change in GDH1, leading to a 2fold enhanced oxidative deamination
ADP
-
activates in presence of 3 M NaCl or 3 M KCl or in absence of salts
ADP
-
1 mM, approx. 2fold activation of membrane-bound liver enzyme
ADP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
AMP

-
-
AMP
-
1 mM, reaction velocity increases 15fold at saturating NAD+ and glutamate levels
AMP
-
activates NADH-linked glutamate synthesis, inhibits NADPH-linked activity
AMP
-
activation only in biosynthetic direction
ATP

-
-
ATP
-
4.8fold activation, cofactor 0.08 mM NADH
ATP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
ATP
-
wild-type: activation at 1 mM, inhibition below and above, H454Y and S448P mutant enzymes: progressive increase in activity until 10 mM, inhibition above
ATP
-
activates in presence of 3 M NaCl or in absence of salts, slight inhibition in presence of 3 M KCl
ATP
-
approx. 1.5fold activation of membrane-bound liver enzyme
ATP
-
allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
GTP

-
inhibition at pH 9.0, activation in presence of electrolytes at pH 6.0
L-Leu

0.3-10 mM stimulates isoenzyme GLUD2 to a greater extent than isoenzyme GLUD1
L-Leu
0.3-10 mM stimulates isoenzyme GLUD2 to a greater extent than isoenzyme GLUD1. In absence of GTP the isoenzyme GLUD2 assumes a conformational state associated with little catalytic activity, it remains amenable to full activation by ADP and/or L-Leu
L-Leu
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-leucine

-
allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 725% activation by L-leucine, respectively. Activation of NAD+ and NADP+ reduction by 40% and 135%, respectively
L-leucine
-
L-leucine displays the same affinity for hGDH2 and hGDH1
leucine

-
wild-type, S448P, H454Y and R463A mutant enzymes
leucine
-
the enzyme is subject to allosteric activation by leucine invlving ARg134, and Asp185, structural mechanism, overview
leucine
with 10 mM the activity increases by 1.55fold after 240 min and by 1.24fold when the enzyme is preincubated with methylglyoxal
leucine
enhances the oxidative deamination reaction of GDH1
leucine
-
the enzyme is subject to allosteric activation by leucine, structural mechanism, overview
leucine
-
activates at 5°C only
additional information

-
not inhibited by trypsin
-
additional information
-
serum GLDH activity is elevated in alcohol abuse
-
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0.00294
alpha-ketoglutarate
-
-
0.291
N6-(2-aminoethyl)-NAD+
-
-
0.273
N6-(2-aminoethyl)-NADP+
-
-
0.148
N6-(2-hydroxy-2-trimethylammoniumpropyl)-NAD+
-
-
0.052
N6-(3-sulfonatopropyl)-NAD+
-
-
0.444
poly(ethyleneglycol)-N6-(2-aminoethyl)-NAD+
-
-
-
0.425
poly(ethyleneglycol)-N6-(2-aminoethyl)-NADP+
-
-
-
additional information
additional information
-
0.1
2-oxoglutarate

-
euthermic animal, assay at 37°C
0.14
2-oxoglutarate
-
NADP-linked reductive amination
0.18
2-oxoglutarate
-
reductive amination, low-activity form of the enzyme
0.2
2-oxoglutarate
-
cosubstrate NADPH
0.2
2-oxoglutarate
-
reductive amination, high-activity form of the enzyme
0.2
2-oxoglutarate
pH 7.6, 70°C, recombinent enzyme (unheated)
0.25
2-oxoglutarate
-
NADPH-dependent activity
0.25
2-oxoglutarate
-
concentration range: 0.3-4.0 mM
0.25
2-oxoglutarate
pH 7.6, 70°C, native enzyme
0.3
2-oxoglutarate
pH 7.6, 70°C, recombinent enzyme (heated)
0.36
2-oxoglutarate
-
NADH + NH4Cl
0.36
2-oxoglutarate
-
isozyme 1, amination activity, cofactor NADH
0.4
2-oxoglutarate
-
50 mM Tris-HCl, pH 7.2
0.43
2-oxoglutarate
-
hibernating animal, assay at 5°C
0.47
2-oxoglutarate
-
NADPH + NH4Cl
0.53
2-oxoglutarate
-
pH 7.6, 90°C
0.59
2-oxoglutarate
-
isozyme 3, amination activity, cofactor NADH
0.6
2-oxoglutarate
-
cosubstrate NADH
0.62
2-oxoglutarate
-
glutamate dehydrogenase 2, 0.1 mM NADH
0.63
2-oxoglutarate
-
NADPH-dependent amination
0.64
2-oxoglutarate
-
NADPH-dependent amination
0.7
2-oxoglutarate
-
cofactor NADH
0.7
2-oxoglutarate
-
NADPH-dependent amination
0.98
2-oxoglutarate
-
hibernating animal, assay at 37°C
1
2-oxoglutarate
-
liver enzyme
1.1
2-oxoglutarate
-
glutamate dehydrogenase 2, 80 mM NH4+
1.16
2-oxoglutarate
-
mutant C274G, hGDH1
1.2
2-oxoglutarate
-
500 mM Tris-HCl, pH 7.2
1.23
2-oxoglutarate
-
isozyme 2, amination activity, cofactor NADH
1.25
2-oxoglutarate
-
25°C, wild-type enzyme
1.25
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme
1.25
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH1
1.25
2-oxoglutarate
-
hGDH1, wild-type
1.25
2-oxoglutarate
-
wild-type, hGDH1
1.25
2-oxoglutarate
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
1.25
2-oxoglutarate
-
wild type isozyme GDH1, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.27
2-oxoglutarate
-
mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.29
2-oxoglutarate
-
25°C, mutant enzyme K333L
1.29
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187E
1.29
2-oxoglutarate
-
mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.31
2-oxoglutarate
-
25°C, mutant enzyme K344L
1.31
2-oxoglutarate
-
25°C, mutant enzyme K346L
1.31
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187M
1.34
2-oxoglutarate
-
hGDH1, mutant C323L
1.34
2-oxoglutarate
-
mutant C59G, hGDH1
1.36
2-oxoglutarate
-
hGDH1, mutant C323Y
1.36
2-oxoglutarate
-
mutant C59Y, hGDH1
1.37
2-oxoglutarate
-
mutant C274Y, hGDH1
1.38
2-oxoglutarate
-
hGDH1, mutant C323M
1.39
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH2
1.39
2-oxoglutarate
-
hGDH1, mutant C323R
1.39
2-oxoglutarate
-
hGDH2, wild-type
1.39
2-oxoglutarate
-
wild-type, hGDH2
1.39
2-oxoglutarate
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
1.39
2-oxoglutarate
-
wild type isozyme GDH2, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
1.4
2-oxoglutarate
-
assay at 37°C
1.4
2-oxoglutarate
-
pH 7.6, 60°C
1.4
2-oxoglutarate
-
hGDH1, mutant C323G
1.4
2-oxoglutarate
-
mutant C274A, hGDH1
1.4
2-oxoglutarate
-
mutant C59A, hGDH1
1.41
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
1.41
2-oxoglutarate
-
hGDH2, mutant C323Y
1.44
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187R
1.45
2-oxoglutarate
-
25°C, mutant enzyme K337L
1.45
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187G
1.45
2-oxoglutarate
-
hGDH2, mutant C323L
1.45
2-oxoglutarate
-
hGDH2, mutant C323M
1.46
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme Y187S
1.47
2-oxoglutarate
-
25°C, mutant enzyme S445L
1.5
2-oxoglutarate
-
25°C, mutant enzyme G446D
1.5
2-oxoglutarate
-
hGDH2, mutant C323R
1.5
2-oxoglutarate
-
mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
1.5 - 2
2-oxoglutarate
-
hGDH2, mutant C323G
1.51
2-oxoglutarate
-
glutamate dehydrogenase 1, 400 mM NH4+
1.51
2-oxoglutarate
-
glutamate dehydrogenase 1, 0.1 mM NADH
1.54
2-oxoglutarate
-
isozyme 1, amination activity, cofactor NADPH
1.58
2-oxoglutarate
-
mutant C274G, hGDH2
1.58
2-oxoglutarate
-
mutant C59Y, hGDH2
1.59
2-oxoglutarate
-
mutant C274A, hGDH2
1.61
2-oxoglutarate
-
mutant C59A, hGDH2
1.66
2-oxoglutarate
-
mutant C274Y, hGDH2
1.67
2-oxoglutarate
-
mutant C59G, hGDH2
1.73
2-oxoglutarate
-
isozyme 3, amination activity, cofactor NADH
1.85
2-oxoglutarate
-
isozyme 2, amination activity, cofactor NADPH
1.86
2-oxoglutarate
-
mutant C119Y, hGDH1
1.9
2-oxoglutarate
-
mutant C119A, hGDH1
1.94
2-oxoglutarate
-
mutant C119G, hGDH1
2
2-oxoglutarate
-
wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
2.1
2-oxoglutarate
-
cosubstrate NADPH
2.1
2-oxoglutarate
-
glutamate dehydrogenase 1, 40 mM NH4+
2.1
2-oxoglutarate
-
wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
2.12
2-oxoglutarate
-
mutant C119A, hGDH2
2.18
2-oxoglutarate
-
mutant C119G, hGDH2
2.26
2-oxoglutarate
-
mutant C119Y, hGDH2
2.3
2-oxoglutarate
-
kidney enzyme
2.6
2-oxoglutarate
-
glutamate dehydrogenase 1, 0.2 mM NADPH
3.13
2-oxoglutarate
-
25°C, mutant enzyme H454Y
3.3
2-oxoglutarate
-
cosubstrate NADH
3.5
2-oxoglutarate
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
3.66
2-oxoglutarate
-
euthermic animal, assay at 5°C
3.7
2-oxoglutarate
-
glutamate dehydrogenase 1, 0.2 mM NADH
3.7
2-oxoglutarate
-
glutamate dehydrogenase 2, 0.2 mM NADPH
4
2-oxoglutarate
-
cofactor NADPH
4.5
2-oxoglutarate
-
cofactor NADH
5
2-oxoglutarate
-
NADH-dependent activity
6.3
2-oxoglutarate
-
cofactor NADPH
7.1
2-oxoglutarate
-
pH 8.0
7.1
2-oxoglutarate
-
NAD-linked reductive amination
10.5
2-oxoglutarate
-
assay at 5°C
14
2-oxoglutarate
-
500 mM Tris-HCl, pH 8.2
0.25
glutamate

-
hibernating animal, assay at 5°C
0.32
glutamate
-
concentration range: 0.05-1.0 mM
0.47
glutamate
-
assay at 5°C
0.5
glutamate
-
euthermic animal, assay at 5°C
2.03
glutamate
-
euthermic animal, assay at 37°C
2.6
glutamate
-
assay at 37°C
4.61
glutamate
-
mitochondrial enzyme, cofactor NAD+
5.2
glutamate
-
hibernating animal, assay at 37°C
5.5
glutamate
-
concentration range: 1.0-10.0 mM
5.93
glutamate
-
enzyme from rough ER, cofactor NAD+
12
glutamate
-
cosubstrate NAD+
20.7
glutamate
-
mitochondrial enzyme, cofactor NADP+
23.8
glutamate
-
enzyme from rough ER, cofactor NADP+
0.24
L-glutamate

-
at pH 8.5
0.3
L-glutamate
-
cosubstrate NAD+
0.3
L-glutamate
-
pH 8.0, 70°C
0.4
L-glutamate
-
kidney enzyme
0.6
L-glutamate
-
pH 7.6, 90°C
0.64
L-glutamate
-
isozyme 1, deamination activity
1
L-glutamate
-
1 mM, NAD+
1.01
L-glutamate
-
at pH 7.4
1.1
L-glutamate
-
cosubstrate NADP+
1.6
L-glutamate
-
cofactor NADP+
1.66
L-glutamate
-
cofactor NAD+
1.7
L-glutamate
-
50 mM Tris-HCl, pH 7.2
1.77
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
1.81
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH2
2.4
L-glutamate
-
NADP-linked oxidative deamination
2.5
L-glutamate
-
pH 7.6, 60°C
2.98
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
3
L-glutamate
-
1 mM, NADP+
3
L-glutamate
-
isozyme 3, deamination activity
3
L-glutamate
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
3.44
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme
3.44
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH1
3.52
L-glutamate
-
isozyme 2, deamination activity
3.65
L-glutamate
-
oxidative deamination, low-activity form of the enzyme
3.71
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
3.76
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279M
3.83
L-glutamate
-
oxidative deamination, high-activity form of the enzyme
3.94
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279Y
3.98
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279G
4.05
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279L
4.12
L-glutamate
-
pH 9.5, 25°C, mutant enzyme E279R
5.51
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
7.3
L-glutamate
-
NAD-linked oxidative deamination
7.99
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
10
L-glutamate
-
NADP+-dependent activity
10.41
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
10.7
L-glutamate
-
wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
10.8
L-glutamate
-
mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
12.4
L-glutamate
-
wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
17.75
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
19.5
L-glutamate
-
500 mM Tris-HCl, pH 9.4
21.82
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
25
L-glutamate
-
0.004 mM, NAD+
25.82
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
30.55
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
31
L-glutamate
-
500 mM Tris-HCl, pH 7.2
0.014
NAD+

-
-
0.016
NAD+
-
50 mM Tris-HCl, pH 7.2
0.02
NAD+
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
0.032
NAD+
-
kidney enzyme
0.063
NAD+
-
+ L-glutamate
0.1
NAD+
-
pH 8.0, 25°C, recombinant enzyme
0.11
NAD+
-
500 mM Tris-HCl, pH 9.4
0.11
NAD+
-
pH 8.0, 25°C, native enzyme
0.15
NAD+
-
500 mM Tris-HCl, pH 7.2
0.2
NAD+
-
isozyme 1, deamination activity
0.26
NAD+
-
isozyme 2, deamination activity
0.32
NAD+
-
isozyme 3, deamination activity
0.364
NAD+
-
mitochondrial enzyme
0.43
NAD+
-
oxidative deamination, low-activity form of the enzyme
0.53
NAD+
-
substrate L-glutamate
0.55
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
0.58
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
0.59
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH2
0.63
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
0.65
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
0.71
NAD+
-
pH 9.5, 25°C, wild-type enzyme
0.71
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH1
0.75
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
0.76
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
0.79
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
0.82
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
0.92
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
0.924
NAD+
-
enzyme from rough ER
0.94
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
2.44
NAD+
-
oxidative deamination, high-activity form of the enzyme
3
NAD+
-
NAD-linked oxidative deamination
6.94
NAD+
-
pH 9.5, 25°C, mutant enzyme E279G
7.6
NAD+
-
pH 9.5, 25°C, mutant enzyme E279R
8.35
NAD+
-
pH 9.5, 25°C, mutant enzyme E279Y
9.98
NAD+
-
pH 9.5, 25°C, mutant enzyme E279M
10.01
NAD+
-
pH 9.5, 25°C, mutant enzyme E279L
0.000175
NADH

-
-
0.004
NADH
-
50 mM Tris-HCl, pH 7.2
0.007
NADH
-
+ 2-oxoglutarate
0.009
NADH
-
glutamate dehydrogenase 1, 5 mM 2-oxoglutarate
0.009
NADH
-
glutamate dehydrogenase 2, 5 mM 2-oxoglutarate
0.01
NADH
-
500 mM Tris-HCl, pH 8.2
0.012
NADH
-
glutamate dehydrogenase 2, 80 mM NH4+
0.012
NADH
-
500 mM Tris-HCl, pH 7.2
0.015
NADH
-
liver enzyme
0.02
NADH
-
glutamate dehydrogenase 1, 40 mM NH4+
0.022
NADH
-
kidney enzyme
0.04
NADH
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
0.048
NADH
-
glutamate dehydrogenase 1, 400 mM NH4+
0.05
NADH
-
glutamate dehydrogenase 1, 12.5 mM 2-oxoglutarate
0.07
NADH
-
isozyme 1, amination activity, cofactor NADH
0.075
NADH
-
mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.076
NADH
-
25°C, mutant enzyme K346L
0.079
NADH
-
25°C, mutant enzyme K333L
0.08
NADH
-
pH 8.0, 25°C, wild-type enzyme
0.08
NADH
-
mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.081
NADH
-
25°C, wild-type enzyme
0.081
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH1
0.081
NADH
-
hGDH1, wild-type
0.081
NADH
-
wild-type, hGDH1
0.081
NADH
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
0.081
NADH
-
wild type isozyme GDH1, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.082
NADH
-
pH 8.0, 25°C, mutant enzyme Y187E
0.082
NADH
-
pH 8.0, 25°C, mutant enzyme Y187R
0.083
NADH
-
pH 7.6, 90°C
0.084
NADH
-
pH 8.0, 25°C, mutant enzyme Y187M
0.085
NADH
-
pH 8.0, 25°C, mutant enzyme Y187G
0.086
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH2
0.086
NADH
-
hGDH2, wild-type
0.086
NADH
-
wild-type, hGDH2
0.086
NADH
-
isozyme GDH2, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
0.086
NADH
-
wild type isozyme GDH2, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
0.088
NADH
-
25°C, mutant enzyme K337L
0.088
NADH
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
0.088
NADH
-
pH 8.0, 25°C, mutant enzyme Y187S
0.089
NADH
-
25°C, mutant enzyme G446D
0.09
NADH
-
isozyme 3, amination activity, cofactor NADH
0.09
NADH
-
concentration range: 0.04-0.1 mM
0.09
NADH
-
25°C, mutant enzyme K344L
0.09
NADH
-
mutant C119A, hGDH1
0.091
NADH
-
mutant C119Y, hGDH1
0.092
NADH
-
mutant C119G, hGDH1
0.094
NADH
-
mutant C59G, hGDH1
0.097
NADH
-
mutant C59A, hGDH1
0.098
NADH
-
25°C, mutant enzyme S445L
0.098
NADH
-
mutant C119G, hGDH2
0.099
NADH
-
mutant C59A, hGDH2
0.099
NADH
-
mutant C59Y, hGDH1
0.101
NADH
-
mutant C119A, hGDH2
0.102
NADH
-
mutant C59Y, hGDH2
0.106
NADH
-
mutant C59G, hGDH2
0.108
NADH
-
mutant C119Y, hGDH2
0.117
NADH
-
hGDH1, mutant C323L
0.119
NADH
-
hGDH1, mutant C323G
0.119
NADH
-
hGDH1, mutant C323M
0.119
NADH
-
hGDH2, mutant C323M
0.121
NADH
-
hGDH2, mutant C323L
0.122
NADH
-
25°C, mutant enzyme H454Y
0.122
NADH
-
hGDH1, mutant C323R
0.125
NADH
-
hGDH2, mutant C323R
0.128
NADH
-
hGDH2, mutant C323G
0.129
NADH
-
hGDH1, mutant C323Y
0.13
NADH
-
reductive amination, low-activity form of the enzyme
0.138
NADH
-
hGDH2, mutant C323Y
0.14
NADH
-
isozyme 2, amination activity, cofactor NADH
0.14
NADH
-
pH 7.6, 50°C
0.169
NADH
-
mutant C274A, hGDH2
0.175
NADH
-
mutant C274G, hGDH2
0.176
NADH
-
mutant C274Y, hGDH2
0.178
NADH
-
mutant C274Y, hGDH1
0.181
NADH
-
mutant C274G, hGDH1
0.189
NADH
-
mutant C274A, hGDH1
0.2
NADH
-
NAD-linked reductive amination
0.5
NADH
-
NADH-dependent activity
0.52
NADH
-
reductive amination, high-activity form of the enzyme
0.98
NADH
-
substrate 2-oxoglutarate
0.004
NADP+

-
NADP+-dependent activity
0.013
NADP+
-
oxidative deamination, low-activity form of the enzyme
0.019
NADP+
-
NADP-linked oxidative deamination
0.025
NADP+
-
+ L-glutamate
0.025
NADP+
-
pH 7.6, 90°C
0.028
NADP+
-
cosubstrate glutamate
0.029
NADP+
-
oxidative deamination, high-activity form of the enzyme
0.035
NADP+
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
0.08
NADP+
-
concentration range: 0.02-0.2 mM
0.1
NADP+
-
pH 8.0, 70°C
0.18
NADP+
-
substrate L-glutamate
0.31
NADP+
-
cosubstrate norvaline
0.443
NADP+
-
enzyme from rough ER
0.637
NADP+
-
mitochondrial enzyme
0.006
NADPH

-
NADPH-dependent amination
0.01
NADPH
-
+ 2-oxoglutarate
0.01
NADPH
-
pH 7.6, 60°C
0.011
NADPH
-
reductive amination, low-activity form of the enzyme
0.013
NADPH
-
NADPH-dependent activity
0.013
NADPH
-
NADP-linked reductive amination
0.013
NADPH
-
reductive amination, high-activity form of the enzyme
0.018
NADPH
-
NADPH-dependent amination
0.02
NADPH
-
NADPH-dependent amination
0.028
NADPH
-
glutamate dehydrogenase 1, 10 mM 2-oxoglutarate
0.028
NADPH
-
glutamate dehydrogenase 2, 10 mM 2-oxoglutarate
0.037
NADPH
-
pH 7.6, 90°C
0.04
NADPH
-
concentration range: 0.002-0.1 mM
0.04
NADPH
pH 7.6, 70°C, native enzyme
0.05
NADPH
pH 7.6, 70°C, recombinent enzyme (heated)
0.069
NADPH
-
glutamate dehydrogenase 1, 40 mM NH4+
0.069
NADPH
-
glutamate dehydrogenase 2, 80 mM NH4+
0.1
NADPH
pH 7.6, 70°C, recombinent enzyme (unheated)
0.17
NADPH
-
50 mM Tris-HCl, pH 7.2
0.27
NADPH
-
isozyme 1, amination activity, cofactor NADPH
0.46
NADPH
-
isozyme 3, amination activity, cofactor NADPH
0.54
NADPH
-
500 mM Tris-HCl, pH 7.2
0.56
NADPH
-
substrate 2-oxoglutarate
0.56
NADPH
-
substrate NH3
0.75
NADPH
-
500 mM Tris-HCl, pH 8.2
0.78
NADPH
-
isozyme 2, amination activity, cofactor NADPH
0.38
NH3

-
biphasic Lineweaver-Burk plot suggests 2 Km values
1.25
NH3
-
reductive amination, high-activity form of the enzyme
1.31
NH3
-
reductive amination, low-activity form of the enzyme
1.5
NH3
-
NADPH-dependent amination
1.7
NH3
-
NADP-linked reductive amination
2.4
NH3
-
NADPH-dependent amination
2.5
NH3
pH 7.6, 70°C, recombinent enzyme (unheated)
2.9
NH3
-
NADPH-dependent amination
4.9
NH3
-
NAD-linked reductive amination
5.1
NH3
-
NADP-linked reductive amination
10
NH3
-
in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C
11.4
NH3
pH 7.6, 70°C, recombinent enzyme (heated)
12.8
NH3
-
hGDH1, pH 8.0, temperature not specified in the publication
13
NH3
pH 7.6, 70°C, native enzyme
13.4
NH3
-
wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
14.7
NH3
-
hGDH2, pH 8.0, temperature not specified in the publication
17.1
NH3
-
wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
22.2
NH3
-
mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP
33
NH3
-
hGDH2, pH 7.5, temperature not specified in the publication
35
NH3
-
hGDH1, pH 7.5, temperature not specified in the publication
44
NH3
-
NADPH + 2-oxoglutarate
50
NH3
-
NADH + 2-oxoglutarate
57.5
NH3
-
hGDH1, pH 7.0, temperature not specified in the publication
62.2
NH3
-
hGDH2, pH 7.0, temperature not specified in the publication
66
NH3
-
NADH-dependent activity
100
NH3
-
biphasic Lineweaver-Burk plot suggests 2 Km values
0.0424
NH4+

-
-
1.3
NH4+
-
concentration range: 0.2-5 mM
2.82
NH4+
-
pH 7.6, 90°C
5.8
NH4+
-
glutamate dehydrogenase 1, 0.2 mM NADPH
7
NH4+
-
glutamate dehydrogenase 1, 0.2 mM NADPH
7
NH4+
-
euthermic animal, assay at 37°C
10.4
NH4+
-
glutamate dehydrogenase 1, 10 mM 2-oxoglutarate
12.1
NH4+
-
hibernating animal, assay at 5°C
12.9
NH4+
-
glutamate dehydrogenase 2, 5 mM 2-oxoglutarate
13
NH4+
-
isozyme 2, amination activity, cofactor NADH
13
NH4+
-
concentration range: 10-200 mM
15
NH4+
-
cosubstrates NADPH + 2-oxoglutarate
15.8
NH4+
-
glutamate dehydrogenase 1, 5 mM 2-oxoglutarate
15.8
NH4+
-
hibernating animal, assay at 37°C
17.8
NH4+
-
assay at 37°C
19
NH4+
-
glutamate dehydrogenase 1, 10 mM 2-oxoglutarate
21.7
NH4+
-
glutamate dehydrogenase 1, 0.1 mM NADH
22.8
NH4+
-
glutamate dehydrogenase 1, 0.1 mM NADH
24.7
NH4+
-
euthermic animal, assay at 5°C
27
NH4+
-
cosubstrates NADH + 2-oxoglutarate
30
NH4+
-
isozyme 1, amination activity, cofactor NADH
36
NH4+
-
isozyme 1, amination activity, cofactor NADPH
41
NH4+
-
isozyme 3, amination activity, cofactor NADPH
44
NH4+
-
isozyme 3, amination activity, cofactor NADH
53
NH4+
-
isozyme 2, amination activity, cofactor NADPH
58
NH4+
-
500 mM Tris-HCl, pH 8.2
77
NH4+
-
500 mM Tris-HCl, pH 7.2
106
NH4+
-
glutamate dehydrogenase 1, 12.5 mM 2-oxoglutarate
115.1
NH4+
-
glutamate dehydrogenase 1, 0.2 mM NADH
160
NH4+
-
50 mM Tris-HCl, pH 7.2
additional information
additional information

-
-
-
additional information
additional information
-
Km-values for 2-oxoglutaratefor mutant enzyme R443S, recombinant wild-type enzyme and wild-type enzyme from human liver
-
additional information
additional information
kinetic analysis in wild-type and transgenic overexpressing brain cell fractions, overview
-
additional information
additional information
-
kinetic analysis in wild-type and transgenic overexpressing brain cell fractions, overview
-
additional information
additional information
-
lowering the pH of the buffer from pH 8.0 to pH 7.0 increases the Km for ammonia substantially, i.e. for hGDH1 from 12.8 mM to 57.5 mM, and for hGDH2: from 14.7 mM to 62.2 mM, thus essentially precluding reductive amination
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
14
2-oxoglutarate

-
hGDH1, mutant C323Y
15
2-oxoglutarate
-
hGDH1, mutant C323R
17
2-oxoglutarate
-
hGDH1, mutant C323G
17
2-oxoglutarate
-
hGDH1, mutant C323L
17
2-oxoglutarate
-
hGDH2, mutant C323Y
19
2-oxoglutarate
-
hGDH1, mutant C323M
19
2-oxoglutarate
-
hGDH2, mutant C323M
19
2-oxoglutarate
-
hGDH2, mutant C323R
20
2-oxoglutarate
-
hGDH2, mutant C323L
21
2-oxoglutarate
-
hGDH2, mutant C323G
104
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH1
104
2-oxoglutarate
-
hGDH1, wild-type
130
2-oxoglutarate
-
pH 8.0, 25°C, wild-type enzyme hGDH2
130
2-oxoglutarate
-
hGDH2, wild-type
134
2-oxoglutarate
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
165.3
2-oxoglutarate
-
pH 7.6, 90°C
183
2-oxoglutarate
-
cofactor NADH
195
2-oxoglutarate
-
concentration range: 0.3-4.0 mM
510
2-oxoglutarate
-
reduction
25
glutamate

-
oxidation
40
glutamate
-
concentration range: 0.05-1.0 mM
61
glutamate
-
cofactor NADP+
162
glutamate
-
concentration range: 1.0-10.0 mM
714
glutamate
-
cofactor NADH, + 1 mM ADP
2
L-glutamate

-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
3.33
L-glutamate
-
cofactor NAD+, value below 200.0
4
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
4.83
L-glutamate
-
cofactor NAD+
11
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
14
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
42
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
48
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
57
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
57
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
57
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
59
L-glutamate
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
65
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH1
83
L-glutamate
-
pH 9.5, 25°C, wild-type enzyme hGDH2
121.2
L-glutamate
-
pH 7.6, 90°C
2
NAD+

-
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
4
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
11
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
14
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
42
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1G96Y
48
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1K118Y
51
NAD+
-
pH 9.5, 25°C, mutant enzyme E279M
57
NAD+
-
pH 9.5, 25°C, mutant enzyme E279L
57
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH1D172Y
57
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2D172Y
57
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2G96Y
59
NAD+
-
pH 9.5, 25°C, mutant enzyme E279G
59
NAD+
-
pH 9.5, 25°C, mutant enzyme hGDH2K118Y
61
NAD+
-
pH 9.5, 25°C, mutant enzyme E279R
65
NAD+
-
pH 9.5, 25°C, wild-type enzyme
65
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH1
68
NAD+
-
pH 9.5, 25°C, mutant enzyme E279Y
83
NAD+
-
pH 9.5, 25°C, wild-type enzyme hGDH2
77
NADH

-
mutant C119G, hGDH1
79
NADH
-
mutant C119Y, hGDH1
81
NADH
-
mutant C119A, hGDH1
85
NADH
-
mutant C59Y, hGDH1
88
NADH
-
mutant C274Y, hGDH1
90
NADH
-
concentration range: 0.04-0.1 mM
90
NADH
-
mutant C274A, hGDH1
90
NADH
-
mutant C59A, hGDH1
91
NADH
-
mutant C274G, hGDH1
91
NADH
-
mutant C59G, hGDH1
93
NADH
-
25°C, mutant enzyme K333L
95
NADH
-
25°C, mutant enzyme H454Y
98
NADH
-
25°C, mutant enzyme K337L
100
NADH
-
25°C, mutant enzyme K346L
100
NADH
-
mutant C274Y, hGDH2
101
NADH
-
mutant C119G, hGDH2
101
NADH
-
mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
102
NADH
-
25°C, mutant enzyme G446D
103
NADH
-
mutant C119Y, hGDH2
104
NADH
-
25°C, wild-type enzyme
104
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH1
104
NADH
-
wild-type, hGDH1
104
NADH
-
isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
104
NADH
-
wild type isozyme GDH1, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
105
NADH
-
25°C, mutant enzyme K344L
105
NADH
-
mutant C119A, hGDH2
108
NADH
-
mutant C59Y, hGDH2
109
NADH
-
mutant C274G, hGDH2
110
NADH
-
mutant C59G, hGDH2
111
NADH
-
25°C, mutant enzyme S445L
114
NADH
-
mutant C274A, hGDH2
117
NADH
-
mutant C59A, hGDH2
118
NADH
-
mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
130
NADH
-
pH 8.0, 25°C, wild-type enzyme hGDH2
130
NADH
-
wild-type, hGDH2
130
NADH
-
isozyme GDH2, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C
130
NADH
-
wild type isozyme GDH2, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C
134
NADH
-
pH 8.0, 25°C, mutant enzyme S443R hGDH2
374.5
NADH
-
pH 7.6, 90°C
102
NADP+

-
concentration range: 0.02-0.2 mM
399.6
NADP+
-
pH 7.6, 90°C
112
NADPH

-
concentration range: 0.002-0.1 mM
200
NADPH
-
NADPH-dependent activity