Th1L07 Enzymes (FC)

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Medicine Y1 (Theme 1 | Cells and organelles) Flashcards on Th1L07 Enzymes (FC), created by Emma Allde on 17/08/2016.
Emma Allde
Flashcards by Emma Allde, updated more than 1 year ago
Emma Allde
Created by Emma Allde over 8 years ago
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Question Answer
Oxidoreductases add O2 or remove 2H
Lactase dehydrogenase is what kind of enzyme oxidoreductase
Transferases transfer of function groups from donors to acceptors a way of producing non-essential amino acids and moving around carbon skeletons and nitrogen
Hydrolases hydrolytic reactions
Trypsin is what kind of enzyme hydrolase
Isomerases isomerisation reactions catalyse the transfer of functional groups within the same molecule
Ligases form C-C or C-N-bonds with ATP cleavage to catalyse the formation of new covalent bonds the loss of a phosphate group (going one way)
Alcohol dehydrogenase is what kind of enzyme oxidoreductase E.C. 1.1.1.1
What do enzyme active sites contain that stabile the reaction functional groups
Lock and Key hypothesis the first enzyme model not perfect Enzyme has two substrates that it tries to bring together to interact
Induced Fit Model Unfilled binding site suggests that the enzyme alters the shape of a substrate to make it more suitable for a reaction
Where does pepsin work + at what pH is it most effective Enzyme in the stomach; most effective around pH of 2
Where does trypsin work + at what pH is it most effective Enzyme in the digestive system (intestines); most effective around pH of 6
Where does alkaline phosphate work + at what pH is it most effective Enzyme in the bloodstream; most effective around pH of 8
What are isoenzymes Enzymes with different protein structures which catalyse the same reaction Found in different cellular compartments (cytoplasm or mitochondria) because they have different biochemical roles
Are isoenzymes coded for by different enzymes yes
Hexokinase/ glycokinase are examples of what isoenzymes
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