Enzymes

Question 1

• are catalysts and are not consumed in the reactions
• are proteins that act as a catalyst for biochemical reactions

Answer 1

Enzymes

Question 2

composed only of protein (amino acid chains)

Answer 2

Simple enzyme

Question 3

• is the protein part of the enzyme which lacks the cofactor.
• is catalytically inactive and incomplete and determines the specificity of this system for
  a substrate.

Answer 3

Apoenzyme

Question 4

Has a nonprotein part in addition to a protein part.

Answer 4

Conjugated enzyme

Question 5

• are important for the chemically reactive enzymes
• are small organic molecules or Inorganic ions

Answer 5

cofactor

Question 6

is the biochemically active conjugated enzyme

Answer 6

holoenzyme

Question 7

Enzymes are grouped into 6 major classes based on the types of reactions they catalyze

Answer 7

1. Oxidoreductases
2. Transferases
3. Hydrolases
4. Lyases
5. Isomerase
6. Ligases

Question 8

 Oxidation and reduction reactions are always linked to one another
 An ____________ requires a coenzyme that is either oxidized or reduced as the substrate in the reaction.

Answer 8

Oxidoreductase

Question 8

• catalyze transfer of a phosphate group from adenosine triphosphate (ATP) to a substrate

Answer 8

Kinases

Question 8

• catalyze transfer of an amino group to a substrate

Answer 8

Transaminases

Question 9

A _____________ is an enzyme that catalyzes the transfer of a functional group from one molecule to another
 Two major subtypes:
Transaminases
Kinases

Answer 9

Transferase

Question 10

• A ______________ is an enzyme that catalyzes a hydrolysis reaction
• The reaction involves addition of a water molecule to a bond to cause bond breakage

Answer 10

hydrolase

Question 11

A ________ is an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

Answer 11

Lyase

Question 12

 effects the removal of the components of water from a double bond

Answer 12

Dehydratase

Question 13

 effects the addition of the components of water to a double bonds

Answer 13

Hydratase

Question 14

An ____________ is an enzyme that catalyzes the isomerization (rearrangement of atoms) reactions.

Answer 14

Isomerase

Question 15

A _________ is an enzyme that catalyzes the formation of a bond between two molecules involving ATP hydrolysis

Answer 15

Ligase

Question 16

 An enzyme will catalyze a particular reaction for only one substrate
 This is most restrictive of all specificities (not common)

Answer 16

Absolute Specificity

Question 17

 An enzyme can distinguish between stereoisomers.
 Chirality is inherent in an active site (amino acids are chiral compounds)

Answer 17

Stereochemical Specificity

Question 18

 Involves structurally similar compounds that have the same functional groups.

Answer 18

Group Specificity

Question 19

 Involves a particular type of bond irrespective of the structural features in the vicinity of the bond
 Considered most general of enzyme specificities

Answer 19

Linkage Specificity

Question 20

• the condition of participating in or catalyzing only one or a few chemical reactions

Answer 20

SPECIFICITY

Question 21

• a modification and especially increase in the rate of a chemical reaction induced by material unchanged chemically at the end of the reaction.

Answer 21

CATALYSIS

Question 22

• a region on the surfa e of an enzyme whose shape permits binding only of a specific molecular substrate that then undergoes catalysis.

Answer 22

ACTIVE SITE

Question 22

- relating to, undergoing, or being a change in the shape and activity of protein (such as enzyme) that results from combination with another substance at a point other than the chemically activie site.

Answer 22

ALLOSTERIC SITE

Question 23

Accidently discovered by Alexander Fleming in 1928

Answer 23

Penicillins

Question 24

Considered the best broad-spectrum antibiotics because it is effective against skin and bone infections as well as against infections involving the urinary, gastrointestinal, and respiratory systems

Answer 24

Cipro

Question 25

A process in which enzyme activity is altered by covalently modifying the structure of the enzyme

Answer 25

Covalent modification

Question 26

 Some regulators increase enzyme activity

Answer 26

activators

Question 26

process in which activation or inhibition of the first reaction in a reaction sequence is controlled by a product of the reaction sequence.

Answer 26

Feedback Control

Question 26

Cellular processes continually produces large amounts of an enzyme and plentiful amounts of products if the processes are not regulated.

Answer 26

Regulation of Enzyme Activity

Question 26

 Some regulators decrease enzyme activity

Answer 26

inhibitors

Question 27

An irreversible enzyme inhibitor inactivates enzymes by forming a strong covalent bond with the enzyme’s active site

Answer 27

Irreversible Inhibition

Question 28

A noncompetitive enzyme inhibitor decreases enzyme activity by binding to a site on an enzyme other than the active site.

Answer 28

Reversible Noncompetitive Inhibition

Question 29

resembles an enzyme substrate in shape and charge

Answer 29

competitive enzyme inhibitor

Question 30

a substance that slows down or stops the normal catalytic function of an enzyme by binding to it.

Answer 30

Enzyme Inhibitor

Question 31

Enzymes are not consumed in the reactions they catalyze

Answer 31

Enzyme Concentration

Question 32

At a constant enzyme concentration, the enzyme activity increases with increased substrate concentration

Answer 32

Substracte Concentration

Question 33

the concentration at which it reaches its maximum rate and all of the active sites are full

Answer 33

Substrate saturation

Question 34

Number of substrate molecules converted to product per second per enzyme molecule under conditions of optimum temperature and pH

Answer 34

Turnover Number