Table 1 Kinetic parameters of the enzymes in the second part of the glycolysis.

From: Identification of flux checkpoints in a metabolic pathway through white-box, grey-box and black-box modeling approaches

Enzyme

Kma

Kia

Keqa

Vmaxa

kcatb

Ec

PGAM

473 (3PG)

106 (2PG)

173 (PPi)

 

Vf = 75

Vr = 67.24

kcat_f = 3,420

kcat_r = 3,066.14

2.19*10–2

ENO

86.4 (2PG)

102 (PEP)

137 (PPi)

610 (3PG)

 

Vf = 328.5

Vr = 66.61

kcat_f = 8,820

kcat_r = 1,788.43

3.72*10–2

PPDK

30 (PEP)

2 (AMP)

91 (PPi)

221 (Pyr)

597 (ATP)

1,342 (Pi)

 

0.73

Vf= 196.5

Vr = 12.28

kcat_f = 5,220

kcat_r = 326.22

3.76*10–2

  1. Michaelis constants (Km) and inhibitor constants (Ki) are in µM, maximum rates of the forward and reverse reactions (Vf and Vr) in mU, enzyme amounts (E) in nmol and kcat of the forward and reverse reactions (kcat_f and kcat_r) in min−1. Keq is the equilibrium constant of the reaction.
  2. aData taken from a previous study8 and Vr were calculated from enzyme proportions7.
  3. bData taken from a previous study6 and kcat_r were calculated from Vr and E.
  4. cE were calculated from Vf and kcat_f by using the equation: \(E = \frac{{V}_{f}}{{k}_{cat\_f}}\).
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