Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Michaelis-Menten kinetics of single enzymes

In Chapter 4 (Section 4.1.1), we derived the Lineweaver-Burk double-reciprocal relation between the steady state flux of an enzyme reaction and its substrate concentrations. (See Equation (4.5).) Furthermore, we showed in Section 4.4.1 that the same equation can be obtained from a stochastic point of view. Recalling this derivation, consider the basic mechanism [Pg.270]

Breaking down the overall reaction of converting one S to one P, the first step of binding of S to E takes an average time l/( i[S]). The dwell time in state ES is + k2), after which the ES complex transitions either to E + P or back to [Pg.270]


See other pages where Michaelis-Menten kinetics of single enzymes is mentioned: [Pg.270]   


SEARCH



Enzyme kinetic

Enzyme kinetics

Kinetic of enzymes

Kinetics of enzymes

MENTEN

Menten kinetics

Michaelis enzyme kinetics

Michaelis kinetics

Michaelis-Menten

Michaelis-Menten enzyme

Michaelis-Menten enzyme kinetic

Michaelis-Menten enzyme kinetics

Michaelis-Menten kinetic

Michaelis-Menten kinetics

© 2024 chempedia.info