Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0055 | - |
guanosine 5'-phosphate | pH 7.8, 25°C | Escherichia coli | |
0.0147 | - |
NADPH | pH 7.8, 25°C | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37382 | - |
4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry | Escherichia coli |
37383 | - |
4 * 38000, SDS-PAGE, 4 * 37383, calculated | Escherichia coli |
37384 | - |
4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry | Escherichia coli |
38000 | - |
4 * 38000, SDS-PAGE, 4 * 37383, calculated | Escherichia coli |
38000 | - |
4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry | Escherichia coli |
156000 | - |
gel filtration | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
IMP + NH3 + NADP+ = GMP + NADPH + H+ | ordered bi-bi kinetic mechanism, in which GMP binds first to the enzyme followed by NADPH binding, and NADP+ dissociates first followed by IMP release. GMP and IMP binding are thermodynamically favorable processes. Hydride transfer contributes to the rate-limiting step, and protonation and hydride transfer steps take place in the same transition state, lending support to a concerted mechanism. Product release does not contribute to the rate-limiting step of the reaction | Escherichia coli | |
IMP + NH3 + NADP+ = GMP + NADPH + H+ | ordered bibi kinetic mechanism, in which GMP binds first to the enzyme followed by NADPH binding, and NADP+ dissociates first followed by IMP release | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.66 | - |
pH 7.8, 25°C | Escherichia coli |
Storage Stability | Organism |
---|---|
-80°C, no loss of activity | Escherichia coli |
-80°C, stable | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
NADPH + guanosine 5'-phosphate | - |
Escherichia coli | NADP+ + inosine 5'-phosphate + NH3 | GMP and IMP binding are thermodynamically favorable processes. Protonation and hydride transfer steps take place in the same transition state. Product release does not contribute to the rate-limiting step of the reaction | ? | |
NADPH + H+ + guanosine 5'-phosphate | - |
Escherichia coli | NADP+ + inosine 5'-phosphate + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 4 * 38000, SDS-PAGE, 4 * 37383, calculated | Escherichia coli |
tetramer | 4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
guaC | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.28 | - |
guanosine 5'-phosphate | pH 7.8, 25°C | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no cofactor: NADH | Escherichia coli | |
additional information | no activity detected with NADH or adenosine 5'-phosphate | Escherichia coli | |
NADPH | - |
Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
19 | - |
NADPH | pH 7.8, 25°C | Escherichia coli | |
51 | - |
guanosine 5'-phosphate | pH 7.8, 25°C | Escherichia coli |