Enzymes - Bioprocess Engineering: Kinetics, Biosystems, Sustainability and Reactor Design - page 349

r P

r

max

No inhibition

r max

r max ' =

1 + [ I]
K I

Uncompetitive inhibition

1
2 r max

1
2 '

r max

[S] = K m

[S] = K ( 1 + )

[I]

K I

m

0

0

[S]

FIGURE 8.13 Comparison of Michaelis e Menten and uncompetitive inhibition enzyme kinetics.

r P

No inhibition

Substrate inhibition

0

S max

0

[S]

FIGURE 8.14 Comparison of substrate inhibited and uninhibited enzymatic reactions.

K m ¼ ½

E ½ S

(8.67)

½

ES

K S 2 ¼ ½

ES ½ S

(8.68)

½ ES

2

½ E 0 ¼½ E þ½ ES þ½ ES 2

and

r p ¼ k 2 ½ ES (8.70)