Michaelis-Menten kinetics of enzymes, the concept of 'perfect' enzymes with some examples, and a brief overview of serine proteases, ATP synthase and topoismoerases
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Created by Hannah Tribe
over 10 years ago
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Close
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Created by Hannah Tribe
over 10 years ago
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Name 5 functions of enzymes
What is the Vmax and how is it achieved?
What is the Michaelis constant (Km) and how is it achieved?
The binding of enzyme with substrate is limited by _________ and cannot really be changed by evolution.
The conversion of the enzyme-substrate complex to the product can be improved by evolution. The _______ of the enzyme can be changed to improve conversion to products.
What is a 'perfect' enzyme?
When an enzyme is 'perfect', the reaction is said to be _________ ________. The rate of these reactions is approx. ____^__ M-1 s-1.
How can the rate of the reaction be calculated using the Michaelis-Menten kinetics?
How can k3 be calculated?
Name 1 enzyme which is near 'perfect'
How can it be tested experimentally to see if an enzyme is 'perfect'? Which enzyme was this first tested on?
What do serine proteases do and why are they so efficient?
Name 3 serine proteases and where they are produced
What do they all have at their active site, which is responsible for the reactive serine residue?
How is this enzyme pathway different to the uncatalysed pathway?
Chymotrypsin can only cleave to bonds following __________ side chains (e.g. Phenylalanine, Tryptophan, Tyrosine).
Trypsin can only cleave to bonds following _________ chains (e.g. Lysine, Arginine).
Elastase can only cleave to bonds following _____ side chains.
Name 2 molecular machines
How does ATP synthase work?
How does topoisomerase II work?
