enzymes

Question 1

what are enzymes

Answer 1

are tertiary structured proteins which speed up rate of reaction without getting used up themselves

Question 2

how do enzymes lower activation energy?

Answer 2

they bend the bonds in the substrate putting a strain on the bonds and making them more likely to break
or
they bring molecules close together overcoming natural repulsion between two molecules making the bond more likely

Question 3

what’s the induced fit

Answer 3

the active site is complementary shape to the substrate but not perfectly
when the substrate binds it causes a slight change to the active site
this change bends the bonds in the substrate causing them to break more rapidly

Question 4

what is the active sites shape maintained by?

Answer 4

the bonds in the enzymes tertiary structure
the change in active site is seen as denaturing

Question 5

how does temperature affect enzyme activity

Answer 5

it increases the kinetic energy of the enzyme and substrate. they are more likely to collide and form enzyme substrate complexes
above optimum temp the H bonds in the tertiary structure break and the active site changes so is no longer complementary
The hydrogen bonds between the h of the amino group and o of the carboxyl group

Question 6

how does Ph affect enzyme activity

Answer 6

away from the optimum the ionic bonds between R groups break. the active site then changes shape and is no longer complementary to the substrate
enzyme substrate complexes above optimum then cannot form

Question 7

how does substrate or enzyme concentration affect rate of reaction

Answer 7

as the concentration of both increases the rate increases. this is due to more collisions and an increase in enzyme-substrate complex. at high concentrations the rate levels off as there is a limiting factor

Question 8

competitive inhibitors

Answer 8

an inhibitor is the same shape as a substrate which means it can fit and bind to the active site. it blocks the real substrate from bunching however an increase in substrate concentration overcomes the inhibitor.

Question 9

what’s a non competitive inhibitor

Answer 9

binds to the allosteric site causing a change in shape of active site so is no longer complementary. it is irreversible