Flashcards
Th1L07 Enzymes (FC)
Cards in this deck (17)
- 1Oxidoreductasesadd O2 or remove 2H
- 2Lactase dehydrogenase is what kind of enzymeoxidoreductase
- 3Transferasestransfer of function groups from donors to acceptors
a way of producing non-essential amino acids and moving around carbon skeletons and nitrogen - 4Hydrolaseshydrolytic reactions
- 5Trypsin is what kind of enzymehydrolase
- 6Isomerasesisomerisation reactions
catalyse the transfer of functional groups within the same molecule - 7Ligasesform 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) - 8Alcohol dehydrogenase is what kind of enzymeoxidoreductase
E.C. 1.1.1.1 - 9What do enzyme active sites contain that stabile the reactionfunctional groups
- 10Lock and Key hypothesisthe first enzyme model
not perfect
Enzyme has two substrates that it tries to bring together to interact - 11Induced Fit ModelUnfilled binding site suggests that the enzyme alters the shape of a substrate to make it more suitable
for a reaction - 12Where does pepsin work + at what pH is it most effectiveEnzyme in the stomach; most effective around pH of 2
- 13Where does trypsin work + at what pH is it most effectiveEnzyme in the digestive system (intestines); most effective around pH of 6
- 14Where does alkaline phosphate work + at what pH is it most effectiveEnzyme in the bloodstream; most effective around pH of 8
- 15What are isoenzymesEnzymes with different protein structures which catalyse the same reaction
Found in different cellular compartments (cytoplasm or mitochondria) because
they have different biochemical roles - 16Are isoenzymes coded for by different enzymesyes
- 17Hexokinase/ glycokinase are examples of whatisoenzymes
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- User has deleted their subject information Flashcards on Th1L07 Enzymes (FC), created by Deleted user on 26/08/2016.
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- Deleted user · Aug 2016
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- Aug 27, 2016
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- Created by Emma Allde · Aug 17, 2016
- Copied by Emma Allde · Aug 26, 2016
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