Competitive and uncompetitive enzyme inhibition
In the stated reversible single-substrate Michaelis–Menten model, competitive inhibition increases apparent Km while leaving Vmax unchanged.
Key knowledge
In the stated reversible single-substrate Michaelis–Menten model, competitive inhibition increases apparent Km while leaving Vmax unchanged. Uncompetitive binding to the enzyme–substrate complex reduces both apparent Km and Vmax by the same factor. Observed patterns constrain a kinetic model without uniquely locating every molecular binding site.
Values and equations
Competitive: v=Vmax[S]/(Km(1+[I]/Ki)+[S])
- v,Vmax
- initial and limiting reaction rates mol m⁻³ s⁻¹
- [S],[I]
- substrate and inhibitor concentrations mol m⁻³
- Km,Ki
- Michaelis and inhibitor dissociation constants mol m⁻³
Conditions and scope
- Use initial-rate conditions and the stated reversible binding assumptions.
- Mixed inhibition and irreversible inactivation require other models; allosteric and noncompetitive are not synonyms.
Sources · 1
References
Sources retain their recorded scope. A source link alone does not establish verification of every statement.
Evidence and review
Read competitive and uncompetitive equations and mechanistic qualifications, printed pp. 10–12.
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Entry details
Permanent link to this entry ↗- Record identity
- uni-bio-competitive-inhibition
- Revision
- core.1
- Structured reference record
- University core expansion