cofactors and coenzymes Flashcards
define coenzyme
organic cofactor not permanently attached to the protein
define cofactor
non-protein component necessary for effective functioning of an enzyme (ions or organic molecules)
describe the similarities between cofactors, coenzymes and prosthetic groups.
- coenzymes and prosthetic groups are both cofactors
- cofactors and prosthetic groups can be organic or inorganic
describe differences between cofactors, coenzymes and prosthetic groups.
- coenzymes are organic cofactors - not permanently attached to the protein
- prosthetic groups are cofactors that are permanently attached to the enzyme
why is the chloride ion necessary for the correct formation of the amylase active site is a cofactor, not a coenzyme or prosthetic group
- it is organic (coenzymes are organic)
- it is not permanently attached (prosthetic groups are)
explain why zinc ions that form an important part of the structure of carbonic anhydrase is a prosthetic group, not a cofactor or coenzyme.
- it is permanently attached (stating cofactor is ambiguous as they are both)
- inorganic (coenzymes are organic only)
give two examples of coenzymes synthesised from vitamins in our diet.
- NAD (vitamin B3)
- NADP (vitamin B3)
define inorganic precursor enzyme
enzyme that requires biochemical change for it to become active
explain why inactive precursor enzymes may be produced
- to prevent enzymes from causing damage within the cells producing them when released
- when enzymes action needs to be controlled
describe 3 ways in which inactive precursor may be activated.
- adding a cofactor
- action of another enzyme
- change in conditions
define apoenzyme
protein that forms an active enzyme by combination with a cofactor
define holoenzyme
active form of an enzyme
define zymogens
inactive enzymes that require a biochemical change (change in conditions/acted on by another enzyme) to become an active enzyme.
define proenzymes
inactive enzymes that require a biochemical change (change in conditions/acted on by another enzyme) to become an active enzyme.
give 2 examples of inactive precursor enzymes and describe how they are activated
- pepsinogen: becomes pepsin when exposed to stomach acid (low pH)
- trypsinogen: becomes trypsin when cleaved into active form by enteropeptidase