Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Homo sapiens | |
ADP | - |
Bos taurus | |
additional information | no activation by ADP | [Clostridium] symbiosum |
Crystallization (Comment) | Organism |
---|---|
crystal structure determination and analysis | [Clostridium] symbiosum |
Protein Variants | Comment | Organism |
---|---|---|
D165H | site-directed mutagenesis, catalytically inactive mutant | [Clostridium] symbiosum |
additional information | site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview | Homo sapiens |
additional information | site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview | Bos taurus |
W243F | site-directed mutagenesis, catalytically impaired enzyme due to hindered glutamate binding, the mutant shows Michaelis-Menten kinetics | [Clostridium] symbiosum |
W310F | site-directed mutagenesis, the mutant shows Michaelis-Menten kinetics | [Clostridium] symbiosum |
W393F | site-directed mutagenesis | [Clostridium] symbiosum |
W449F | site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme | [Clostridium] symbiosum |
W64F | site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme | [Clostridium] symbiosum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
GTP | - |
Bos taurus | |
GTP | - |
Homo sapiens | |
additional information | no inhibition by GTP | [Clostridium] symbiosum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | cofactor kinetics, overview | Homo sapiens | |
additional information | - |
additional information | cofactor kinetics, overview | Bos taurus | |
additional information | - |
additional information | cofactor kinetics, overview. Even without the heterotropic antenna responsible for allosteric regulation in mammalian enzymes, the GDH is emphatically still allosteric. The Eadie-Hofstee plot for NAD+ is strongly non-linear.Att pH 9.0 there is almost total positive co-operativity with glutamate, with a Hill coefficient close to the theoretical maximum of 6 for a hexamer | [Clostridium] symbiosum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | Homo sapiens | - |
2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NAD+ | Bos taurus | - |
2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NAD+ | [Clostridium] symbiosum | - |
2-oxoglutarate + NH3 + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Homo sapiens | - |
- |
- |
[Clostridium] symbiosum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | - |
Homo sapiens | 2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NAD+ | - |
Bos taurus | 2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NAD+ | - |
[Clostridium] symbiosum | 2-oxoglutarate + NH3 + NADH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
GDH | - |
Homo sapiens |
GDH | - |
Bos taurus |
GDH | - |
[Clostridium] symbiosum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Homo sapiens | |
NAD+ | - |
Bos taurus | |
NAD+ | - |
[Clostridium] symbiosum | |
NADH | - |
Homo sapiens | |
NADH | - |
Bos taurus | |
NADH | - |
[Clostridium] symbiosum |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the family of amino acid dehydrogenases | Homo sapiens |
evolution | the enzyme belongs to the family of amino acid dehydrogenases | Bos taurus |
evolution | the enzyme belongs to the family of amino acid dehydrogenases | [Clostridium] symbiosum |
metabolism | together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP | Homo sapiens |
metabolism | together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP | Bos taurus |
additional information | Trp243 is located in the active-site cleft. Neither Trp64 nor Trp449 are strictly required for pH-dependent inactivation | [Clostridium] symbiosum |
physiological function | complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites | Homo sapiens |
physiological function | complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites | Bos taurus |
physiological function | CsGDH lacks the regulation by ADP and GTP seen in bovine GDH | [Clostridium] symbiosum |