Enzymes Mechanism Of Actiom

Question 1

Why are enzymes preferred over inorganic catalysts?

Answer 1

Greater specificity(no side products), milder ruxn conditions, higher reaction rates, can be regulated

Question 2

Oxidoreductase

Answer 2

Transfer of electrons (H atoms)

Question 3

Transferases

Answer 3

Group transfer

Question 4

Hydrolases

Answer 4

Hydrolysis. Transfer of functional groups to water

Question 5

Lyases

Answer 5

Cleavage of c-c,c-o,c-n or other bonds by elimination, leaving double bonds

Question 6

Isomerases

Answer 6

Transfer of groups within molecules to yield isomeric forms

Question 7

Ligases

Answer 7

Formation of c-c,c-o,c-n, c-s bonds by condensation coupled to cleavage of ATP

Question 8

Prosthetic groups

Answer 8

Tightly and stably incorporated into proteins structure by covalent or noncovalent forces

Question 9

Cofactors

Answer 9

Bind in a transient, dissociable manner either to enzyme or to a substrate such as ATP (metal ions)

Question 10

Coenzymes

Answer 10

Group transfer agents and transport many substrates from one point within the cell to another

Question 11

Apoenzyme

Answer 11

Enzyme without the factor

Question 12

Holoenzyme

Answer 12

Complete enzyme with prosthetic group

Question 13

Deficiency of niacin

Answer 13

Causes pellagra. Vitamin form of NAD and NADP

Question 14

Tetrahydrofolate

Answer 14

Donates a carbon in amino and nucleic acid synthesis in the form of CH2, CH2OH, or CHO)
Deficiency:low birth weight,spina bifida

Question 15

Catalysis by proximity

Answer 15

Effective molarity and orientation of substrate molecules in active site of enzymes will enhance rate of rxn

Question 16

acid-base catalysis

Answer 16

Ionizable functional groups of amino acid side chains and prosthetic groups contribute to catalysis by acting as acids or bases

Question 17

Catalysis by strain

Answer 17

Enzymes bind their substrates in an unfavorable conformation to weaken the bond to be cleaved

Question 18

Covalent catalysis

Answer 18

Form covalent bind between enzyme and one or more substrates to create a more reactive enzyme. (Group transfer)

Question 19

Isozymes

Answer 19

Multiple enzymes for catalyze she of same reaction.

Differ in rxn rate, inhibition, mobility, immunologic properties.

Question 20

Coenzyme Lipoate

Answer 20

Transfer electrons and acyl groups, not in diet

Question 21

Tetrahydrofolate

Answer 21

Transfers one carbon groups, in Folate, deficiency causes spina bifida

Question 22

Thiamin pyrophosphate (TPP)

Answer 22

Vitamin is thiamin B1.
Involved in aldehyde transfers
In lentil, brown rice, cereal.
Causes beriberi if deficient

Question 23

a-lipoid acid (lipoamide)

Answer 23

Not a vitamin, acyl group transfer, tomatoes broccoli spinach, no deficiency symptoms

Question 24

Coenzyme A

Answer 24

• Vitamin pantothenic acid (B5)
• acyl group transfer
• chicken yogurt avocados
• no deficiency

Question 25

Nicotinamide adenine dinucleotide (NAD+)

Answer 25

In Niacin (B3)
Redox rxn (hydride ions)
Poultry, fish, veggies
Causes pellagra when deficienct

Question 26

Flavin Adenine Dinucleotiden(FAD)

Answer 26

Riboflavin (B2)
Redox rxn(electron transport)
Dairy, almonds, asparagus
Cheilosis (swelling, cracked lips)

Question 27

Serum enzyme Aminotransferases
y-glutamyl transferase
Lactate dehydrogenase isozyme 5

Answer 27

Major diagnostic use is Liver diseases

Question 28

Serum Amylase and Lipase

Answer 28

Acute pancreatitis

Question 29

Serum creative kinase

Answer 29

Muscle disorders and myocardial infarction

Question 30

Phosphatase

Answer 30

Acid is metastatic carcinoma of prostate,

Basic is bone disorders and obstructive liver diseases