EC Number   |
Metals/Ions |
Reference |
|---|
    6.3.5.4 | Br- |
can partially replace Cl- in activation |
1713 |
| 6.3.5.4 | Br- |
strong activation of Asn synthesis and Gln hydrolysis. The synthetase reactions with NH3 or NH2OH are only slightly stimulated |
1678 |
| 6.3.5.4 | Ca2+ |
at 16.7 mM CaCl2 31% of the activation relative to MgCl2 |
1674 |
| 6.3.5.4 | Cl- |
required for glutaminase and glutamine-dependent synthetase activity, not for the NH4+-dependent activity |
1713 |
| 6.3.5.4 | Cl- |
required, Km: 1.7 mM |
1688 |
| 6.3.5.4 | Cl- |
stimulation of the Gln-dependent reaction and glutaminase reaction. Inhibition of the NH4+-dependent reaction, competitive with respect to NH4+, with negative cooperativity |
1674 |
| 6.3.5.4 | Cl- |
strong activation of Asn synthesis and Gln hydrolysis, competitive activator with respect to Gln and a noncompetitive activator with respect to MgATP2- and Asp. Cl- changes the substrate saturation kinetics of Gln from negatively cooperative to normal hyperbolic and causes a 50fold increase in the affinity for Gln. Inherent glutaminase activity is enhanced 30fold. The synthetase reactions with NH4+ or NH2OH are only slightly stimulated |
1678 |
| 6.3.5.4 | CN- |
stimulates Asn synthesis and Gln hydrolysis |
1678 |
| 6.3.5.4 | Co2+ |
at 16.7 mM CoCl2 31% of the activation relative to MgCl2 |
1674 |
| 6.3.5.4 | Co2+ |
can partially replace Mg2+ in activation |
1709 |
