Enzymes

Question 1

Biological Molecules

Answer 1

Lipids
Carbohydrates
Proteins
Nucleic Acid

Question 2

diverse group of water-insoluble
biological molecules: Fats, Phospholipid and sterols

Answer 2

Lipids

Question 3

Energy stores

Answer 3

Fats

Question 4

major
components of membrane.

Answer 4

Phospholipids and sterols

Question 5

polyhydroxy aldehydes
and ketones with the
general formula of
(CH2O)n.

Answer 5

Carbohydrates

Question 6

most complex and most abundant
organic molecules containing at least one
carboxyl group and one amino group.

Answer 6

Proteins

Question 7

DNA carries coded information,
arranged into genes, that is passed from each
cell to its daughter cells and from one
generation to the next; RNA instrumental in
translating the coded message of DNA into
sequences of amino acids during synthesis of
protein molecules

Answer 7

Nucleic Acid

Question 8

The process of increasing the rate of
reaction with the use of a catalyst.

Answer 8

Catalysis

Question 9

any substance that increases rate
of reaction upon addition to a certain
reaction .

Answer 9

Catalyst

Question 10

catalyst of biochemical reactions (biological
catalysts)

Answer 10

Enzymes

Question 11

lowers
the activation
energy

Answer 11

Enzymes hastens the reaction

Question 12

protein
hydrolysing) hydrolyses any
peptide bond in which the
carbonyl group belongs to a
phenylalanine, tyrosine, or
tryptophan residue.

Answer 12

chymotrypsin (proteolytic
enzyme present in the
intestine)

Question 13

• highly specific nature of most enzymes arises
  from the close and complementary fit between
  enzymes and substrate in a special portion of the
  enzyme surface
• where the substrate can fit like a lock-and-key
  mechanism

Answer 13

Active site

Question 14

catalytic potency
of an enzyme

Answer 14

Enzyme activity

Question 15

number of
reactions catalyzed per second by the
enzyme

Answer 15

Turnover number

Question 16

small organic molecules that
act as cofactors

Answer 16

coenzymes

Question 17

enzyme minus its cofactor;
cannot function without its
cofactor/coenzyme

Answer 17

apoenzyme

Question 18

covalently attached
cofactors, part of the enzyme molecule

Answer 18

vitamins

Question 19

Cofactor (coenzyme, prosthetic group or metal ion) +
apoenzyme =

Answer 19

holoenzyme

Question 20

• used in the living cell as a means of
  controlling enzymatic reactions
• discovered important features of the active
  sites and of the mechanisms of enzyme action
• enzymes can be irreversibly (toxins) or
  reversibly inhibited

Answer 20

enzyme inhibition

Question 21

2 types of enzyme inhibition

Answer 21

competative and noncompetative

Question 22

• caused by molecules
  that react directly with
  the active site of the
  enzyme
• can be reversed by
  an increase in
  substrate
  concentration
  -most competitive
  inhibitors are
  substrate analogs

Answer 22

Competative inhibition

Question 23

• caused by molecules that bind to a region(s)
  of the enzyme outside the active site
• reversed by dilution or removal of the
  inhibitor
• chemical structure of noncompetitive
  inhibitors typically differs from that of the
  substrate.

Answer 23

Noncompetitive inhibition

Question 24

alters the tertiary structure
of the enzyme thus changing the
conformation of the active site

Answer 24

Allosteric site

Question 25

interaction of the end
product occurs in the
allosteric site, making
the end product an _______

Answer 25

Allosteric inhibitor

Question 26

Two kinds of energy yielding metabolic
pathways in animal
tissues:

Answer 26

Aerobic metabolis and Anaerobic metabolism

Question 27

food molecules are
completely oxidized to
carbon dioxide and
water by molecular
oxygen; energy yield is
far greater

Answer 27

Aerobic metabolism

Question 28

food molecules are
oxidized incompletely
to lactic acid (lactate);

• absence of
  oxygen

Answer 28

Anaerobic metabolism