KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | autophosphorylation reaction kinetics, overview. Km values in autophosphorylation of the heme Fe(III)-OH(-), Fe(III)-cyanide, Fe(III)-imidazole, and Fe(II)-O2 bound active AfGcHK forms are 0.0189-00.0354 mM | Anaeromyxobacter sp. Fw109-5 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | 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 | Anaeromyxobacter sp. Fw109-5 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + protein L-histidine | Anaeromyxobacter sp. Fw109-5 | - |
ADP + protein N-phospho-L-histidine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Anaeromyxobacter sp. Fw109-5 | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | autophosphorylation activity | Anaeromyxobacter sp. Fw109-5 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + protein L-histidine | - |
Anaeromyxobacter sp. Fw109-5 | ADP + protein N-phospho-L-histidine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AfGcHK | - |
Anaeromyxobacter sp. Fw109-5 |
globin-coupled histidine kinase | - |
Anaeromyxobacter sp. Fw109-5 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kcat values in autophosphorylation of the heme Fe(III)-OH(-), Fe(III)-cyanide, Fe(III)-imidazole, and Fe(II)-O2 bound active AfGcHK forms are 0.0183-0.02/s | Anaeromyxobacter sp. Fw109-5 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Anaeromyxobacter sp. Fw109-5 | |
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 | Anaeromyxobacter sp. Fw109-5 |
General Information | Comment | Organism |
---|---|---|
additional information | 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. Effects of the response regulator and different divalent metal cations on the autophosphorylation reaction, overview | Anaeromyxobacter sp. Fw109-5 |
physiological function | the globin-coupled histidine kinase, AfGcHK, is a part of the two-component signal transduction system. Activation of its sensor domain significantly increases its autophosphorylation activity, which targets the His183 residue of its functional domain. The phosphate group of phosphorylated AfGcHK is then transferred to the cognate response regulator | Anaeromyxobacter sp. Fw109-5 |