Literature summary for 2.7.13.3 extracted from

Fojtikova, V.; Stranava, M.; Vos, M.H.; Liebl, U.; Hranicek, J.; Kitanishi, K.; Shimizu, T.; Martinkova, M.
Kinetic analysis of a globin-coupled histidine kinase, AfGcHK: effects of the heme iron complex, response regulator, and metal cations on autophosphorylation activity (2015), Biochemistry, 54, 5017-5029.

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KM Value [mM]

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

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Anaeromyxobacter sp. Fw109-5	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	autophosphorylation activity	Anaeromyxobacter sp. Fw109-5

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + protein L-histidine	-	Anaeromyxobacter sp. Fw109-5	ADP + protein N-phospho-L-histidine	-	?

Synonyms

Synonyms	Comment	Organism
AfGcHK	-	Anaeromyxobacter sp. Fw109-5
globin-coupled histidine kinase	-	Anaeromyxobacter sp. Fw109-5

Turnover Number [1/s]

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

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

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

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Release 2023.1 (January 2023)