Skip to main content

Table 1 Thermodynamic parameters associated with binding of cysteine and methionine to OASS

From: Comparative thermodynamic studies on substrate and product binding of O-Acetylserine Sulfhydrylase reveals two different ligand recognition modes

 

Cysteine

Methionine

Temperature

ΔG (kJ/mol)

ΔH (kJ/mol)

TdS (kJ/mol)

ΔG (kJ/mol)

ΔH (kJ/mol)

TdS (kJ/mol)

St OASS binding

      

10°C

-9.6 ± 0.4

-2.7 ± 0.1

6.9

-8.6 ± 0.8

-1.3 ± 0.1

7.3

15°C

-9.6 ± 0.3

-2.8 ± 0.1

6.8

-8.6 ± 0.4

-1.4 ± 0.1

7.2

20°C

-9.8 ± 0.1

-6.4 ± 0.1

3.4

-9.7 ± 0.5

-1.5 ± 0.1

8.2

25°C

-10.6 ± 0.1

-5.9 ± 0.1

4.7

-9.5 ± 0.5

-0.9 ± 0.1

8.6

30°C

-10.2 ± 0.2

-4.4 ± 0.2

5.8

-10.4 ± 0.8

-1.0 ± 0.1

9.4

35°C

-11.0 ± 0.2

-5.4 ± 0.3

5.6

-11.3 ± 1.3

-1.2 ± 0.1

10.1

Hi OASSbinding

      

10°C

-8.3 ± 0.4

-4.6 ± 0.1

3.7

-7.2 ± 0.9

-0.2 ± 0.1

7.1

15°C

-8.7 ± 0.2

-4.6 ± 0.2

4.1

-7.2 ± 0.9

-0.2 ± 0.1

7.5

20°C

-9.5 ± 0.5

-4.4 ± 0.2

5.1

-8.2 ± 1.0

-0.2 ± 0.1

8.0

25°C

-9.5 ± 0.5

-5.4 ± 0.3

4.1

-7.6 ± 1.1

-0.8 ± 0.1

6.9

30°C

-11.0 ± 0.3

-4.5 ± 0.4

6.5

-8.4 ± 1.0

-0.7 ± 0.1

7.7

  1. Titrations were performed in 20 mM Tris buffer (pH 8.0), 50 mM NaCl. Data were fit to a two independent sites binding model that yielded similar values of ΔG, ΔH, and -TΔS for each site.