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Intersections of the three reaction rate expressions provided estimates for the maximal reaction rate and for the threshold lengths, as a function of the Bejan number, the Schmidt number and a catalyst number.
We more simply describe the conversion with a maximal reaction rate α, and concentration of half maximal activity of K α.
Assuming a simple enzyme substrate reaction (Michaelis Menten equation) between thrombin and fibrinogen, the Michaelis constant (Km) value of fibrinogen at 2 g litre−1 (6 µM) represents half of the maximal reaction rate between thrombin and fibrinogen.
Three parameters define HIFα ODD-hydroxylation, the dissociation constant of the PHD/HIFα interaction, K ^ D P ; the maximal reaction rate, ν m a x P ; and the PHD concentration, P tot.
The low activity of the Pk enzyme is solely determined by the generally small value of the maximal reaction rate (rmax = 0.06 mM s-1) as the resulting effector influence (νres) shows a strong activation.
The observed improvements in maximal reaction rate as well as substrate affinity for analogue 8 suggest that the absence of the carbonyl oxygen atom does not hinder metabolite formation by CYP2B6 and may in fact enhance it.
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Forward maximal reaction rates Vmax were set twice as fast as the backward reactions in order to ensure a directed mass flow.
In the case of some mutants, concentrations of NAD(P H required to reach the maximal reaction rates resulted in absorption values exceeding 1 U.
The half-maximal reaction rates are set by m= δ/ g and μ= d/ γ.
The degree of saturation depends on the total amount of reactant available, N= R+ A, relative to the concentrations that give the half-maximal reaction rates, m and μ.
Using model-based estimation, we determined the maximal intrinsic reaction rate of the immobilized amidase completely unmasked from diffusional and carrier acidification effects (vmax, specific) as well as the effective proton diffusion coefficient (Deff,H+).
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