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. Author manuscript; available in PMC: 2007 Jan 29.
Published in final edited form as: Bioorg Chem. 2006 Oct 27;34(6):362–379. doi: 10.1016/j.bioorg.2006.09.001

Table 1.

Kinetic parameters for the inhibition of E1ec by substrate analogues.

Compound Ki (μM) kinact (min−1) kinact/Ki (μM min)−1 Kd (μM)
Acetylphosphinate 0.76 3.34  4.40 0.060a
Acetylphosphinateb 0.12 1.30 10.83 0.005
Acetylphosphinated 0.33 0.55  1.67
Acetylmethylphosphinate 3.33 0.62  0.19 0.10a
Methyl acetylphosphonate 0.199a
2-oxo-3-butynoic acidc 8.5 1.79  0.21 0.20

Ki is the dissociation constant for the initial reversible complex (from kinetic experiment) obtained in the presence of 0.50 mM pyruvate in the incubation mixture.

kinact is the rate constant for conversion of the reversible complex to irreversibly inactivated enzyme

kinact/Ki is the second order rate constant for inactivation

a

Kd is the dissociation constant obtained from CD analysis.

b

Determined from kinetic analysis of inhibition for E. coli PDHc from ref. 16.

c

Determined from kinetic analysis of inhibition for E. coli PDHc from ref. 11,22.

d

Determined from kinetic analysis of inhibition for PDHc from bovine heart from ref 19.