TABLE 3.
Variable | Equivalency |
---|---|
αP | [pyruvate]/KR,Pyr |
cP | KR,Pyr/KT,Pyr |
δ | [NAD]/NADcrit |
η | [ADP]/ADPcrit |
β | [FBP]/KFBP,0.5V |
R | 1 + αP + αN + αPαN |
αN | [NADH]/KR,NADH |
cN | KR,NADH/KT,NADH |
ɛ | [ATP]/ATPcrit |
L | L0 · [(1 + γ)/(1 + β)]m |
γ | [Pi]/KP,0.5V |
T | 1 + cPαP + cNαN + cPαPcNαN |
VR,max, maximum enzyme rate in the R state; L, the equilibrium between the T and R states; KR,Pyr and KT,Pyr, affinity constants for pyruvate in the R and T states, respectively; NADcrit, ADPcrit, and ATPcrit, concentrations of NAD, ADP, and ATP, respectively, at which LDH is expected to be inhibited completely based on the equation of Han and Levenspiel (6); KFBP,0.5V, FBP concentration at which LDH was 50% activated in the absence of Pi; KR,NADH and KT,NADH, affinity constants for NADH in the R and T states, respectively; L0, equilibrium between the T state and the R state of the LDH enzyme without substrate; KP,0.5V, phosphate concentration at which LDH was 50% inhibited, as extrapolated to 0 mM FBP; m and n, number of modulator sites.