EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    6.3.1.2 | -999 |
- |
hydroxylamine |
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60°C, pH 7.8 |
721322 |
| 6.3.1.2 | -999 |
- |
more |
- |
37507, 37560, 37568, 661360 |
| 6.3.1.2 | -999 |
- |
more |
ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity |
37519 |
| 6.3.1.2 | -999 |
- |
more |
enzyme activity is controlled by adenylylation |
37495, 37513 |
| 6.3.1.2 | -999 |
- |
more |
Km for Gln and Glu increases after adenylylation |
37532 |
| 6.3.1.2 | -999 |
- |
more |
Km-values of wild-type and mutant enzymes D50A, D50E, E327A |
37515 |
| 6.3.1.2 | -999 |
- |
more |
Michaelis-Menten kinetics |
744127 |
| 6.3.1.2 | -999 |
- |
more |
the enzymatic rate of GS enzymes shows a hyperbolic curve typical of the enzymes that follow the Michaelis-Menten equation regarding the ATP and glutamate and a sigmoidal curve relative to the hydroxylamine concentration |
746127 |
| 6.3.1.2 | -999 |
- |
more |
the enzyme is modulated by a closed bicyclic covalent interconvertible cascade. It consists of two protein nucleotidylation cycles. One involves the cyclic adenylylation and deadenylylation of glutamine synthetase, the other involves the uridylylation and deuridylylation of Shapiro´s regulatory protein PII |
37497 |
| 6.3.1.2 | -999 |
- |
more |
the site of ADP-ribosylation is Arg172 |
37543 |
