Exam 1 Flashcards
(99 cards)
What is the induced fit model?
as substrate binds to the enzyme, the fit bends so that the substrate induces protein to be the correct shape and allows the reaction to occur
substrate-action-“ase”
ex: glucose phosphorylase
the naming of an enzyme
ex: an enzyme that adds phosphate to glucose
what is an isoenzyme?
a different version of an enzyme made by different organs and tissues that have the same activity
What regulates enzyme activity? (5 factors)
- Mass action: the concentration of substrates and products
- The concentration of enzymes: more enzymes = more binding
- Alteration of enzyme structure: Activation, Temperature, pH
- Cofactors and Coenzymes
- Inhibitors
Law of mass action
reversible reactions will be driven from the
side of the equation where concentration is higher to the side where the concentration is lower
ex: H20+CO2 ⇆ H2CO3
Will adding more substrate increase reaction time?
YES BUT ONLY UNTIL SATURATION: Adding more substrates will increase reaction time until all the enzymes are saturated, meaning there will be a plateau of speed when enzyme is saturated
What will increase the reaction time?
Adding more enzyme
What is the reason behind zymogens?
zymogens are inactive enzymes that are used for urgent processes, like in digestion, to have them in stock when needed
how to activate zymogens?
The part of the polypeptide that is blocking the active site is hydrolyzed “cut” of
What does an enzyme need to bind correctly to a substrate?
correct 3-D shape, correct polar and non-polar groups, correct distribution of charges
What destroys “denatures” an enzyme’s shape?
Heat and Acid (pH)
What are Cofactors?
A mineral that binds to an enzyme that (temporarily) alters the shape to make the active sites available to different substrates
What are Coenzymes?
Organic molecules derived from water-soluble vitamins that make reactions more likely to occur by changing the shape of a substrate
What are Competitive Inhibitors?
a shape that partially fits in the active site that blocks substrate from binding to enzyme
What are Allosteric Inhibitors?
binds to different parts of the enzyme that change its shape meaning that the active site no longer will fit that substrate
What is Ligand?
Something that binds to a binding protien
What are the 3 characteristics that all binding proteins have in common?
- Specificity: bind to a narrow range of ligands
- Saturation: a bigger concentration gradient is not going to affect the speed of reaction
- Competitive Inhibition: alternative ligands will compete with the normal ligand for the active site, therefore, inhibit the normal activity of that binding protein
What are coupled reactions?
Catalysis of one reaction allows the catalysis of a second reaction by a different active site on the same enzyme (both reactions have to occur for either to occur)
What is Exergonic?
[Exer = Out] releases energy, products have less potential energy than the reactants
A –> B + C + heat
heat is a product = energy is released
What is Endergonic?
Requires energy, The products of reaction has more potential energy than the reactants, absorbs free energy from the environment
ex: in cells ATP is usually the source of energy for an endergonic reaction
What is a coupled bioenergetic reaction?
the energy released by the exergonic reaction is used to power the endergonic reaction
What is a spontaneous change?
The released free energy can be harnessed to do work
More free energy (higher G)
less stable and greater work capacity
Less free energy (lower G)
more stable and less work capacity