enzymes

Question 1

activation energy

Answer 1

energy needed to start a chemical reaction (make or break bonds). ATP

Question 2

metabolism

Answer 2

all the chemical reactions that take place in a biological system. anabolism + catabolism

Question 3

anabolism

Answer 3

creates complex molecules

Question 4

catabolism

Answer 4

breaks complex molecules

Question 5

enzyme properties

Answer 5

super specific, usually end in ase, globular, never part of product, used over and over, wear out over time and must be replaced, speeds up chemical reactions, very effective in small amounts, enzyme reactions are reversible - they can easily rip apart the molecule they just made

Question 6

law of mass action

Answer 6

direction of a chemical reaction depends on the concentration of enzyme, reactants and/or products. equilibrium is the goal

Question 7

reactants are called

Answer 7

substrates

Question 8

active site

Answer 8

where substrate binds on an enzyme. here e- are shifted to allow appropriate substrates to bind

Question 9

induced fit model

Answer 9

any number of substrates could be present. enzyme has shape delta d/t binding. enzymes change shape slightly when it binds substrate(s)

Question 10

cofactors

Answer 10

non proteins that assist enzymes, can be organic or inorganic

Question 11

organic cofactors

Answer 11

called coenzymes, usually transfers e-, vitamins/minerals, ex: photosynthesis, cellular respiration

Question 12

inorganic cofactors

Answer 12

metal ions, usually accepts e-, ex: Fe+3, Zn+2

Question 13

enzyme regulation

Answer 13

all enzymes have optimal conditions on which the work best such as ph and temperature

Question 14

pH

Answer 14

most work best at neutral
pepsinogen - stomach (2)
trypsin - in intestines (8.5)

Question 15

temperature

Answer 15

in humans, 98.6 F/ 37 C works best

104 F starts to denature proteins

Question 16

competitive inhibition

Answer 16

substance mimics substrate and binds to active site blocking the real substrate. no product is produced. random and reversible.

Question 17

Poison

Answer 17

Hg, tight permanent bond, irreversible inhibitor, type of competitive inhibition

Question 18

allosteric enzymes

Answer 18

use effectors, allosteric activator - binds to enzyme to make active site form. allosteric inhibitor - binds to enzyme to induce inactive form. binds to special allosteric site on enzyme

Question 19

feedback inhibition

Answer 19

a metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway

Question 20

noncompetitive inhibition

Answer 20

substance binds to site that is not the active site nor an allosteric site causing a shape change that blocks the substrate

Question 21

coupled reaction

Answer 21

endergonic reactions require E input. E usually in the form of of ATP. ex: Na/K pump

Question 22

enzymes and evolution

Answer 22

change 1 bp of DNA and you could get a different shape of protein. new shape means new function