Fundamentals of Enzyme Kinetics¶
Cornish-Bowden, A. (2012). Fundamentals of Enzyme Kinetics. Wiley-Blackwell.
Cited by¶
2 citations across 2 artifacts.
Each citation links to the sentence it supports in the citing article.
Primes¶
- Receptor Saturation
- As Cornish-Bowden (2012) develops in his canonical treatment of cooperative binding and Hill kinetics,
This sourceCanonical enzyme-kinetics reference: develops cooperative binding (Hill coefficient n > 1), allosteric modulation, sigmoidal saturation curves, and how cooperativity steepens the transition from sub-saturation to saturation regimes.
- As Cornish-Bowden (2012) develops in his canonical treatment of cooperative binding and Hill kinetics,
Domain-specific¶
- Enzyme Inhibition
- The mechanism is characterised by four binding modes with clinically distinct kinetic profiles. Competitive inhibition: the inhibitor and substrate compete for the same active site; the inhibitor is displaceable by high substrate concentrations, so Vmax is preserved but Km rises — the dose-response curve shifts rightward and the antagonism is surmountable by higher substrate dose.
This sourceThat competitive inhibition raises apparent Km while leaving Vmax unchanged, so the block is surmountable by raising substrate concentration.
- The mechanism is characterised by four binding modes with clinically distinct kinetic profiles. Competitive inhibition: the inhibitor and substrate compete for the same active site; the inhibitor is displaceable by high substrate concentrations, so Vmax is preserved but Km rises — the dose-response curve shifts rightward and the antagonism is surmountable by higher substrate dose.
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