constant

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Michaelis constant Km = ([k.sub.-1] + [k.sub.2])/[k.sub.1] are used as a measure of substrate affinity to the transporter.
The ratio of the maximum velocity and Michaelis constant give the most precise value for constants [k.sub.1] and [k.sub.4].
where [K.sub.M] is the Michaelis constant and [v.sub.max] is the maximum velocity given by the Michaelis-Menten equation for the uninhibited reaction; S0 denotes the initial concentration of urea; [K.sub.i] and [K.sup.*.sub.i] are the inhibition constants defined as: [K.sub.i] = [E][I]/E[I] and [K.sup.*.sub.i] = [E][I]/(E[I] + [E[I.sup.*]]), respectively [26].
The maximum velocity and apparent Michaelis constant for this reaction was approximately 328.3 units/g wet weight and 2.4 mg/ml starch, respectively.
where [V.sub.c] is the rate of RuBP carboxylation, [V.sub.o] is the rate of RuBP oxygenation, [V.sub.cmax] and [V.sub.omax] are their maximum rates, [K.sub.c] and [K.sub.o] are Michaelis constants for C[O.sub.2] and [O.sub.2], and C and O are, respectively, the concentrations of C[O.sub.2] and [O.sub.2] in the chloroplast stroma.