Term
| Michaelis-Menten Equation |
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Definition
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Term
| Rate of formation of enzyme-substrate complex |
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Definition
ES = K1[E][S] - Formation
ES = (K-1 + K2)[ES] - breakdown |
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Term
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Definition
Substrate concentration at which reaction rate is half of maximal value (1/2 Vmax).
Dissociation constant of ES complex is K2 is much smaller than K-1 |
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Term
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Definition
| 1/Vo = (Km/Vmax * 1/S) + 1/Vmax |
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Term
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Definition
Y intercept - 1/Vmax
X intercept - -1/Km
Slope = Km/Vmax |
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Term
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Definition
| turnover number of an enzyme - number of substrate molecules converted into product by an enzyme molecule in a unit time when enzyme is fully saturated with substrate. Equal to rate constant K2, also called Kcat |
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Term
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Definition
| Tells efficiency of the enzyme by looking at [S]/Km ratio. If [S]<Vo = Kcat/Km * [E][S] |
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Term
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Definition
| Effects only Km, not Vmax. Binds tightly to active sight of enzyme and so substrate cannot get in. Can be overcome by increasing [S] |
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Term
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Definition
| Inhibitor binds to enzyme-substrate complex. Cannot be overcome by addition of more substrate. |
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Term
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Definition
| Inhibitor and substrate can bind simultaneously to enzyme at different binding sites. Decreases turnover number rather than diminishing proportion of ES complex. Cannot be overcome by increasing substrate concentration. |
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Term
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Definition
| Single inhibitor hinders binding of substrate and decreases turnover number |
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