Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-glutamate | a competitive inhibitor against GDH | Synechocystis sp. PCC 6803 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD(P)+ | Synechocystis sp. PCC 6803 | - |
2-oxoglutarate + NH3 + NAD(P)H + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. PCC 6803 | P73684 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD(P)+ | - |
Synechocystis sp. PCC 6803 | 2-oxoglutarate + NH3 + NAD(P)H + H+ | - |
r | |
additional information | the binding affinity of L-glutamate is lower than that of 2-oxoglutarate. Hence, L-glutamate has a weaker affinity than 2-oxoglutarate in binding to the active site of GDH. A comparison of binding site in 2-oxoglutarate and L-glutamate indicate three residues which include Arg401, Trp88, and Arg12 that have important role in interaction between these ligands with active site of GDH | Synechocystis sp. PCC 6803 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
More | sequence comparisons and GDH structure homology modeling studies, overview | Synechocystis sp. PCC 6803 |
Synonyms | Comment | Organism |
---|---|---|
GDH | - |
Synechocystis sp. PCC 6803 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | coenzyme specificity of GDH for NADPH and NADH | Synechocystis sp. PCC 6803 | |
NAD+ | - |
Synechocystis sp. PCC 6803 | |
NADH | - |
Synechocystis sp. PCC 6803 | |
NADP+ | - |
Synechocystis sp. PCC 6803 | |
NADPH | - |
Synechocystis sp. PCC 6803 |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.686 | - |
L-glutamate | pH and temperature not specified in the publication | Synechocystis sp. PCC 6803 |
General Information | Comment | Organism |
---|---|---|
additional information | sequence comparisons and GDH structure homology modeling studies and docking analyses of NADPH, NADH, 2-oxoglutarate, and L-glutamate into the predictive model of GDH, loop modeling, overview | Synechocystis sp. PCC 6803 |