Enzymes

Question 1

Enzymes are predominantly protein in nature with the exception of _____

Answer 1

ribozymes

Question 2

Enzymes increase the rate of a reaction by ___ to ___

Answer 2

10^9 - 10^20

Question 3

Protein part of an enzyme

Answer 3

Apoenzyme

Question 4

Non-protein portion of an enzyme that is necessary for catalytic function

Answer 4

Cofactor

Question 5

Examples of cofactor (2)

Answer 5

Zn2+ and Mg2+

Question 6

Non-protein organic molecule, frequently a B vitamin, that acts as a cofactor

Answer 6

Coenzyme

Question 7

Compound/s whose reaction an enzyme catalyzes

Answer 7

Substrate

Question 8

Specific portion of the enzyme to which a substrate binds during reaction

Answer 8

Active site

Question 9

Any process that initiates or increases the activity of an enzyme

Answer 9

Activation

Question 10

Portion on the enzyme surface where inhibitors/activators bind to regular catalytic reactions

Answer 10

Allosteric site

Question 11

Compounds that slows down the rate of the reaction

Answer 11

Inhibitor

Question 12

Process that makes an active enzyme less active or inactive

Answer 12

Inhibition

Question 13

_____ catalyzes the hydrolysis of peptide bonds formed by the carboxyl group of lysine and arginine

Answer 13

Trypsin

Question 14

Effect of enzyme in the activation energy

Answer 14

Lower activation energy

Question 15

A rigid three-dimensional body where the enzyme surface contains the active site

Answer 15

Lock-and-key model

Question 16

The active site becomes modified to accommodate the substrate

Answer 16

Induced-fit model

Question 17

Classification of enzyme: oxidation-reduction reaction

Answer 17

Oxidoreductases

Question 18

Classification of enzyme: group transfer reactions

Answer 18

Transferases

Question 19

Classification of enzyme: hydrolysis reactions

Answer 19

Hydrolases

Question 20

Classification of enzyme: Addition of two groups to a C-C double bond, or removal of two groups to create a C-C double bone

Answer 20

Lyases

Question 21

Classification of enzyme: isomerization reactions

Answer 21

Isomerases

Question 22

Classification of enzyme: joining to two molecules

Answer 22

Ligases

Question 23

Classification of enzyme: Pyruvate with NADH forms lactate with NAD+ through lactate dehydrogenase

Answer 23

Oxidoreductase

Question 24

Classification of enzyme: Aspartate a-Ketogutarate to Oxaloacetate + Glutamate

Answer 24

Transferase

Question 25

Classification of enzyme: Acetylcholine with H2O to Acetate + Choline through Acetylcholinesterease

Answer 25

Hydrolase

Question 26

Classification of enzyme: cis-Aconitate to Isocitrate through Aconitase

Answer 26

Lyase

Question 27

Classification of enzyme: a-D-Glucose-6-phosphate to a-D-Fructose-6-phosphate through Phosphohexose isomerase

Answer 27

Isomerase

Question 28

Classification of enzyme: ATP + L-tyrosine + tRNA to L-tyrosyl-tRNA + AMP + PP through Tyrosine-tRNA synthetase

Answer 28

Ligase

Question 29

Enzyme activity is affected by (5)

Answer 29

Enzyme concentration Substrate concentration Temperature pH Presence of inhibitors

Question 30

Enzymes made of ribonucleic acid

Answer 30

Ribozymes

Question 31

Three types of inhibitors

Answer 31

Competitive Non-competitive Uncompetitive

Question 32

Type of inhibitor: when it enters the active site, the substrate cannot enter

Answer 32

Competitive

Question 33

Type of inhibitor: the inhibitor binds itself to a site other than the active site (allosterism), thereby changing the conformation of the active site

Answer 33

Noncompetitive

Question 34

Emphasize the shape of the active site (2)

Answer 34

Lock-and-key model and induced-fit model

Question 35

Just ____ amino acids participate in the active site in more than ____ of the enzymes studies to date

Answer 35

5, 65

Question 36

Amino acids that participate in active sites

Answer 36

His, Cys, Asp, Arg, Glu

Question 37

An enzyme-regulation process where the product of a series of enzyme-catalyzed reactions inhibits an earlier reaction in the sequence

Answer 37

Feedback control

Question 38

An inactive form of an enzyme that must have part of its polypeptide chain hydrolyzed and removed before it becomes active

Answer 38

Proenzyme (Zymogen)

Question 39

Example of proenzyme

Answer 39

Trypsin (digestive enzyme)

Question 40

Trypsin is sinthesized and stored as ____, which has no enzyme activity

Answer 40

Trypsinogen

Question 41

Trypsinogen only becomes active only after a six-amino fragment is hydrolyzed and removed from the ______

Answer 41

N-terminal end of its chain

Question 42

Removal of the fragment of trypsinogen changes ____ structure (2)

Answer 42

Primary and tertiary structure

Question 43

Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site

Answer 43

Allosterism

Question 44

Modulation: inhibition of an allosteric enzyme

Answer 44

Negative

Question 45

Modulation: stimulation of allosteric enzyme

Answer 45

Positive

Question 46

A substance that binds to an allosteric enzyme

Answer 46

Regulator

Question 47

The process of affecting enzyme activity by covalently modifying it

Answer 47

Protein modification

Question 48

Best known example of protein modification

Answer 48

Pyruvate kinase inactivated by phosphorylation to pyruvate kinase phosphate

Question 49

An enzyme that occurs in multiple forms; each catalyzes the same reaction

Answer 49

Isoenzyme

Question 50

Example of isoenzyme

Answer 50

Lactas dehydrogenase (LDH) catalyzes the oxidation of lactate to pyruvate

Question 51

Enzyme used for hepatitis

Answer 51

Alanine amino-transferase (ALT)

Question 52

Enzyme used for prostate cancer

Answer 52

Acid phosphatase

Question 53

Enzyme used for Liver or bone disease

Answer 53

Alkaline phosphatase (ALP)

Question 54

Enzyme used for pancreatic disease or mumps

Answer 54

Amylase

Question 55

Enzyme used for heart attack or hepatitis

Answer 55

Aspartate amino-transferase

Question 56

Enzyme used for heart attack (3)

Answer 56

Lactate dehydrogenase (LDH) Creatine phosphokinase (CPK) Phosphohexose isomerase (PHI)

Question 57

A molecule whose shape mimics the transition state of a substrate

Answer 57

Transition state analog

Question 58

Example of transition state analog

Answer 58

Proline racemase reaction (Pyrrole-2-carboxylate mimics the planar transition state)

Question 59

An antibody that has catalytic activity because it was created using a transition state analog as an immunogen

Answer 59

Abzyme