IrreversibleInhibitionA complexcomposed of asubstratebound to theactive site of anenzymeProteinA substance thatreduces the activityof an enzyme byentering the activesite in place of thesubstrate whosestructure it mimics.VmaxA substance thatreduces the activity ofan enzyme by bindingto a location remotefrom the active site,changing itsconformation so that itno longer binds to thesubstrateInhibition that canbe reversedbecause theenzyme inhibitorattaches withweak bondsA specific receptorsite on some partof an enzymemolecule remotefrom the activesiteFactorsthat AffectEnzymeFunctionInducedFitModelA chemicalsubstanceformed as aresult of achemicalreactionSubstrateThis preventsenzymes andproducts from mixing(useful for industrialprocessing, likeremoving lactosefrom milkFeedbackInhibitionProteinFoldingLoss of enzymesecondary, tertiary, orquaternary structure asa result of a change inenvironmental factors(pH/ Temp.) affectingthe ability ofpolypeptides to formbonds with each otherThe maximum numberof chemical conversionsof substrate moleculesper second that a singlecatalytic site willexecute for a givenenzyme concentrationLockand KeyModelFixing enzymesinto a gel or otherimmobilematerials suchthat substratesand wash overthem.ActiveSiteEnzymeMeasure ofaffinity of anenzyme forits substrateEnergyneeded toget areactionstartedpH at whichan enzymeperforms itsactivity thebestCalculatedas close totime zeroas possibleIrreversibleInhibitionA complexcomposed of asubstratebound to theactive site of anenzymeProteinA substance thatreduces the activityof an enzyme byentering the activesite in place of thesubstrate whosestructure it mimics.VmaxA substance thatreduces the activity ofan enzyme by bindingto a location remotefrom the active site,changing itsconformation so that itno longer binds to thesubstrateInhibition that canbe reversedbecause theenzyme inhibitorattaches withweak bondsA specific receptorsite on some partof an enzymemolecule remotefrom the activesiteFactorsthat AffectEnzymeFunctionInducedFitModelA chemicalsubstanceformed as aresult of achemicalreactionSubstrateThis preventsenzymes andproducts from mixing(useful for industrialprocessing, likeremoving lactosefrom milkFeedbackInhibitionProteinFoldingLoss of enzymesecondary, tertiary, orquaternary structure asa result of a change inenvironmental factors(pH/ Temp.) affectingthe ability ofpolypeptides to formbonds with each otherThe maximum numberof chemical conversionsof substrate moleculesper second that a singlecatalytic site willexecute for a givenenzyme concentrationLockand KeyModelFixing enzymesinto a gel or otherimmobilematerials suchthat substratesand wash overthem.ActiveSiteEnzymeMeasure ofaffinity of anenzyme forits substrateEnergyneeded toget areactionstartedpH at whichan enzymeperforms itsactivity thebestCalculatedas close totime zeroas possible

Enzymes - Call List

(Print) Use this randomly generated list as your call list when playing the game. There is no need to say the BINGO column name. Place some kind of mark (like an X, a checkmark, a dot, tally mark, etc) on each cell as you announce it, to keep track. You can also cut out each item, place them in a bag and pull words from the bag.


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  1. Irreversible Inhibition
  2. A complex composed of a substrate bound to the active site of an enzyme
  3. Protein
  4. A substance that reduces the activity of an enzyme by entering the active site in place of the substrate whose structure it mimics.
  5. Vmax
  6. A substance that reduces the activity of an enzyme by binding to a location remote from the active site, changing its conformation so that it no longer binds to the substrate
  7. Inhibition that can be reversed because the enzyme inhibitor attaches with weak bonds
  8. A specific receptor site on some part of an enzyme molecule remote from the active site
  9. Factors that Affect Enzyme Function
  10. Induced Fit Model
  11. A chemical substance formed as a result of a chemical reaction
  12. Substrate
  13. This prevents enzymes and products from mixing (useful for industrial processing, like removing lactose from milk
  14. Feedback Inhibition
  15. Protein Folding
  16. Loss of enzyme secondary, tertiary, or quaternary structure as a result of a change in environmental factors (pH/ Temp.) affecting the ability of polypeptides to form bonds with each other
  17. The maximum number of chemical conversions of substrate molecules per second that a single catalytic site will execute for a given enzyme concentration
  18. Lock and Key Model
  19. Fixing enzymes into a gel or other immobile materials such that substrates and wash over them.
  20. Active Site
  21. Enzyme
  22. Measure of affinity of an enzyme for its substrate
  23. Energy needed to get a reaction started
  24. pH at which an enzyme performs its activity the best
  25. Calculated as close to time zero as possible