Adenylate kinase

Adenylate kinase is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides.

Chemical equation

$ATP + AMP \rightleftharpoons 2ADP$

Rate equation

Reversible mass action rate law is used

$K_{1}[ATP][AMP] - K_{2}[ADP]^2$

Parameter values

Parameter	Value	Organism	Remarks
$K_{1}$	1	HeLa cell line
$K_{2}$	2.26

Parameters with uncertainty

k1=442, k2=1000

The kinetic parameters of adenylate kinase are unknown. Therefore, it was modeled using mass action kinetics with parameters k1 and k2 consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=0.442) is from Bergmeyer H.U. (1974) page 486: $Keq(ATP+AMP \rightarrow 2*ADP, pH=7.4, T=25^oC)=2.26$ Failed to parse (Cannot store math image on filesystem.): \Rightarrow Keq(2*ADP \rightarrow ATP+AMP, pH=7.4, T=25^oC)= \frac{1}{2.26}=0.442 .

Equilibrium constant

Equilibrium constant	Conditions	Source
0.48+/-0.015 (mean+/-SEM; n=7)	pH=7, T=25°C, 10mM Mg2+	NIST database "Thermodynamics of Enzyme-Catalyzed Reactions" entry [61ATK/BUR_640] from Atkinson et al. (1961) Table 2: Therefore, Keq(forward) = 0.48 +/-0.015 (n=7; mean+/-SEM calculated from individual measurements).