Enzymes - Biochemistry
Chemistry
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Sample Data
| Front | What is Michaelis-Menten constant? |
| Back | Km is constant and cannot be changed by changing enzyme or substrate conc. Temp. dependent.At Km half of enzyme sites are occupied.
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| Tags | Biochemistry |
| Front | How is the catalytic efficiency of an enzyme determined? |
| Back | Turnover number (kcat) tells us how fast a single enzyme is able to convert reactants to products.
 kcat and Km are used to determine catalytic efficiency of an enzyme.
 Higher kcat or lower Km --> faster (better) enzymeLower kcat or higher Km --> slower (worse) enzyme |
| Tags | Biochemistry |
| Front | How enzyme and substrate affinity is determined from Km? |
| Back | Lower Km, higher affinity (less S is needed to occupy half of all of the enzymes available).Higher Km is lower affinity. |
| Tags | Biochemistry |