EC Number |
Cofactor |
Reference |
---|
2.7.13.3 | GTP |
this kinase is uniquely specific for GTP in the forward and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP specific histidine kinases, binding structure, modeling, overview |
692901 |
2.7.13.3 | heme |
FixL is an oxygen-binding hemoprotein, the heme domain serves as the dioxygen switch in the FixL/FixJ two-component system |
441730 |
2.7.13.3 | heme |
the Fe(II) heme-bound inactive form has kcat and Km(ATP) values of 0.0067/s and 0.078 mM, respectively, suggesting that its low activity reflects a low affinity for ATP relative to that of the Fe(III) form. The heme-free form exhibits low activity, with kcat and Km(ATP) values of 0.005/s and 0.0336 mM, respectively, suggesting that the heme iron complex is essential for high catalytic activity. The coordination and oxidation state of the sensor domain heme iron profoundly affect the enzyme's catalytic activity because they modulate its ATP binding affinity and thus change its kcat/Km(ATP) value |
740070 |
2.7.13.3 | heme |
the oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity |
441785 |
2.7.13.3 | more |
LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor. Activation of LOVHK by blue-light increases the autophosphorylation activity of the HK domain |
741235 |
2.7.13.3 | more |
no activity with ATP, TTP, or CTP in autophosphorylation |
692901 |
2.7.13.3 | more |
no FAD |
740049 |
2.7.13.3 | more |
non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility |
740869 |