Protein Variants | Comment | Organism |
---|---|---|
G15V | the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP | Escherichia coli |
K331l | the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP | Escherichia coli |
K331R | the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.021 | - |
IMP | wild-type | Escherichia coli | |
0.022 | - |
GTP | wild-type | Escherichia coli | |
0.025 | - |
GTP | mutant G15V | Escherichia coli | |
0.035 | - |
GTP | IMP, mutant G15V | Escherichia coli | |
0.041 | - |
IMP | mutant K331L | Escherichia coli | |
0.047 | - |
IMP | IMP, mutant K331R | Escherichia coli | |
0.28 | - |
Asp | wild-type | Escherichia coli | |
0.35 | - |
Asp | mutant G15V | Escherichia coli | |
0.44 | - |
Asp | GTP, mutant K331R | Escherichia coli | |
0.6 | - |
GTP | mutant K331L | Escherichia coli | |
1.73 | - |
IMP | Asp, mutant K331R | Escherichia coli | |
5.4 | - |
Asp | mutant K331L | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
wild-type and mutant enzymes: G15V, K331L, and K331R | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP | phosphate-binding region of adenylosuccinate synthetase is involved in a conformational change induced by GTP and IMP binding. GTP and IMP binding depend on the presence of the other substrate at the active site of the enzyme | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + IMP + L-Asp | - |
Escherichia coli | GDP + phosphate + adenylosuccinate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia coli |