Enzymes Flashcards
1.7 Enzyme action
catalysts lower activation energy
sucrose+water—>glucose+fructose
S + W must collide with enough energy to alter the arrangement of atoms
free energy of products must be lower than that of substrate
catalyst reduce the minimum energy to activate the reaction
Allow reactions to occur at the low energy of the body
Enzyme structure
a specific region of the enzyme-active site
-small depression within the larger enzyme
molecule on which the enzyme acts on-substrate
-form the enzyme-substrate complex
substrate attaches to enzyme through temporary bonds
Induced fit of enzyme
Active site forms as the E and S interact
change in the environment of the leads to a change in the enzyme
enzyme is flexible. So moulds to the substrate shape
enzyme has a general shape but only gets the specific shape after substrate
1.8 Factors affecting enzyme action
*PH
*Temperature
Measuring enzyme-catalysed reactions (changes from catalysts)
changes from catalysts
-formation of the products of oxygen
-disapearence of a substrate
explanations for enzyme activity
-lot of substrate and no product
-easy for substrate to come into contact with enzymes
-all active sites are filled at any given moment
-amount of substrate decreases and product is increased
-less substrate for active site filling
and products get in the way of filling active site
-longer for substrate to break and products to form. so production of production and the disappearences of substrate tail off.
-graph flatten off bcz all substrate are used up so no new products are formed
measuring rate of change
tangent at point needed to measure rate of change
gradient y2-y2/x2-x1
Effect of temperature on enzyme action
-rise in temp increases the kinetic energy
∴ increase in collisions between S&E
-moe effective collisions
-in a graph it shows a rising curve
-however, high temp causes the H and other bonds to break
∴ causes the proteins to change shape
hence,substrate fits less easilly
so the slope decreases
after higher temp enzyme stop working altogethor
Denaturing
permanent change of enzyme shape
Effect of PH on enzyme action
each enzyme has a optimum PH
PH affects in-alters charges on the active site.S can no longer be attached to A.S
could cause the bond that creats the tertiary structure to break
Effect of enzyme concentration on the rate of reaction
if excess of S, increase of E will cause a increase in products
if there is a limitng number of S, INCREASE in E will not change rate of reactions as nothing is in the AS of the new enzymes
Effects of substrate concentration on the rate of enzyme action
rate of reaction will increase in proportion to the concentration of the S
1.9 Enzyme inhibition
types
Directly or indirectly interfere with the functioning of the active site.
∴ reduce its activity
two types
1. Competitive-bind to active site
2.Non-competitive- bind to enzyme at a position other than the active site
Competitive Inhibitors
Have molecular shape similar to the specific substrate
∴ compete with the substrate for the
available active site
conc of I to conc of S determines the effectiveness
not permanently bound. another molecule takes it place after
eg; succinate (S). malnate(I)
transpeptidase (E) penicillin(I)
Non-competitive inhibitors
Attach to enzyme in places other than the AS
Upon attaching the (I)alters the shape of E
∴ changer the AS.substrate cant attach