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. Author manuscript; available in PMC: 2011 Jun 29.
Published in final edited form as: Biochemistry. 2010 Jun 29;49(25):5377–5389. doi: 10.1021/bi100538b

Table 3.

Kinetic Parameters for Isomerization of GAP by Wildtype and K12G Mutant Yeast Triosephosphate Isomerase.a

Yeast TIM kcatb
S−1
Kmb
mM
kcat/Km
M−1 s−1
Ki for PGA
mM
Wildtype 7300 ± 400 1.1 ± 0.2 6.6 × 106c 0.019 ± 0.004d
K12G 0.6 ± 0.2 50 ± 20 12 ± 0.4 e 1.1 ± 0.2f
Effect g 1.2 × 104 50 5.5 × 105 60
ΔΔG or ΔΔG
kcal/mol
5.6 2.3 7.8 2.4
a

At pH 7.5 (30 mM TEA), 25 °C and I = 0.10 (NaCl). Quoted errors are standard errors obtained from least squares analysis.

b

Determined from the fit of initial velocity data to the Michaelis-Menten equation.

c

Calculated as the ratio of the values of kcat and Km

d

Determined by global nonlinear least squares analysis of initial velocity data in the presence of zero, 21 and 130 µM PGA.

e

Determined as the slope of the plot of vi/[E] against [GAP] for [GAP] ≤ 3 mM (Figure 4, inset).

f

Determined from the nonlinear least squares fit of the data in Figure 5 to eq 7.

g

The effect of the K12G mutation on the kinetic parameter.