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Table 1 Effect of the concentration of ATP and C8D-ATP on the fit of the enzyme kinetic model of hexokinase, acetate kinase, adenylylated GS, deadenylylated GS, phosphofructokinase and shikimate kinase.

From: The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases

Enzyme

ATP : Kinetic model

C8D-ATP: Kinetic model

KIEv max

Shikimate kinase

Michaelis-Menton

Michaelis-Menton

1

v max

2339 ± 600

2433 ± 600

 

K m or K '

0.0065 ± 0.003

0.0128 ± 0.007

 

RMSD a

0.9543

0.9866

 

Hexokinase

Allosteric sigmoidal

Allosteric sigmoidal

1

v max

1226 ± 189

1893 ± 940.7

 

K m or K '

3.263 ± 0.662

4.419 ± 2.749

 

h

1.759 ± 0.207

1.020

 

RMSD a

0.9959

0.9919

 

Acetate kinase

Allosteric sigmoidal

Michaelis-Menton

1

v max

22.29 ± 3.046

19.13 ± 2.103

 

K m or K '

1.323 ± 0.353

1.081 ± 0.289

 

h

1.658 ± 0.302

  

RMSD a

0.9880

0.9704

 

Deadenylylated GS

Allosteric sigmoidal

Allosteric sigmoidal

1

v max

11.49 ± 1.31

13.20 ± 0.651

 

K m or K '

30.88 ± 4.44

6.774 ± 2.331

 

h

3.108 ± 0.316

4.077 ± 0.787

 

RMSD a

0.9972

0.9827

 

PFK b

Allosteric sigmoidal

Allosteric sigmoidal

2

v max

111.3 ± 10.16

45.18 ± 1.012

 

K m or K '

2.265 ± 0.320

0.097 ± 0.031

 

h

1.371 ± 0.098

1.785 ± 0.208

 

RMSD a

0.9982

0.9879

 

Adenylylated GS

Allosteric sigmoidal

Allosteric sigmoidal

>2

v max

8.241 ± 0.787

6.540 ± 0.271

 

K m or K '

15.22 ± 8.776

0.603 ± 0.151

 

h

3.288 ±

3.258 ± 0.589

 

RMSD a

0.9822

0.9924

 
  1. The response of each enzyme to change in the ATP and C8D-ATP concentration was tested for the fit to either an allosteric sigmoidal model or to the Michaelis-Menton model of enzyme kinetics by non-linear regression using the GraphPrism 5 software. The Km or K' were estimated depending on the model. The root mean square deviation of the data from the model is as outlined. The Hill factor for the allosteric sigmoidal model is as indicated. KIEv maxis equal to the KIE attained at ATP and C8D-ATP concentrations at maximum enzyme activities.
  2. a Root mean square deviation of the data defining the kinetic model
  3. b Phosphofructokinase