Enzymes and catalysts

Question 1

Hydrolases

Answer 1

lysis of bonds via addition of water

Question 1

Isomerases

Answer 1

Rearranges bonds to make different isomers

Question 2

Lyases

Answer 2

Lysis of bonds by something OTHER than hydrolysis or oxidation
(if it breaks bonds and doesn’t use water, it’s a lyase)

Question 3

Ligases

Answer 3

Joins carbon atoms together in energy consuming reactions
Will always have ATP as a substrate and two other substrates getting connecting

Question 4

General acids/bases

Answer 4

Glutamate, aspartate, histidine

Question 5

All enzymes that use ATP require

Answer 5

Magnesium

Question 6

Mg helps orient

Answer 6

Phosphate groups on ATP

Question 7

All metal ions are what charge

Answer 7

+ charge

Question 8

Thiamine pyrophosphate

Answer 8

Transfers acyl groups from a-keto acids

Question 9

Acyl

Answer 9

Carbonyl attached to R

Question 10

Acetyl

Answer 10

Carbonyl attached to methyl (CH3)

Question 11

Biotin

Answer 11

Binds CO2 and transfers it as a carboxylate group

Question 12

Pyridoxal phosphate

Answer 12

Transfers amino acids

Question 13

Coenzyme A and lipoic acid

Answer 13

Transfers acyl groups

Question 14

Cobalamin

Answer 14

Transfers methyl groups

Question 15

Tetrahydrofolate

Answer 15

Transfers single carbons

Question 16

Which amino acids can form covalent intermediates

Answer 16

Histidine, lysine, serine, cysteine

Question 17

A smaller y intercept means

Answer 17

High vmax

Question 18

An x intercept closer to 0 means

Answer 18

high km

Question 19

vmax and km of competitive inhibitor

Answer 19

Km increases
Vmax stays the same

Question 20

Vmax and km of uncompetitive inhibitor

Answer 20

Km decreases
vmax decreases

Question 21

vmax and km of noncompetitive inhibitor

Answer 21

km is the same
vmax decreases

Question 22

vmax and km of noncompetitive inhibitors

Answer 22

kmax is the same
vmax decreases

Question 23

In what case does vmax increase

Answer 23

If there’s more enzyme

Question 24

covalent inhibitors modify

Answer 24

Amino acid residues

Question 25

IC50

Answer 25

Inhibitory concentration
In vitro (in parts)

Question 26

EC50

Answer 26

Effective concentration
In vivo (whole tissue)

Question 27

IC50 and EC50 are ______ than Ki

Answer 27

Higher

Question 28

When [S]>km

Answer 28

v0=vmax

Question 29

When [S]<km

Answer 29

v0=vmax/km

Question 30

Three donor and acceptor pairs

Answer 30

NADH:NAD+
FADH2:FAD
Ascorbate:Dehydrascorbate

Question 31

Conditional general acids and bases

Answer 31

Lysine, tyrosine, cysteine, serine, arginine

Question 32

What is NADH and NAD+

Answer 32

NADH: Reducing agent
NAD+” Oxidizing agent

Question 33

What does FADH2 and FAD catalyze

Answer 33

Flavin, Riboflavin B2

Question 34

What does ascorbate: dehydroascorbate catalyze

Answer 34

Vitamin C, fruits, vegetables

Question 35

Acetaldehyde causes

Answer 35

Toxicity
Nausea
Flushing
Vasodilator
Liver damage

Question 36

Ethanol causes

Answer 36

Inebriation
Ataxia
Euphoria

Question 37

Too much acetaldehyde can cause

Answer 37

Metabolic acidosis
Neurological complications

Question 38

Ethylene glycol becomes

Answer 38

Glycol eldehyde
Glycolic acid
Oxalic acid
Calcium oxalate

Question 39

Ethanol becomes

Answer 39

Acetldehyde
Co2 and H2o

Question 40

Methanol becomes

Answer 40

Formaldehyde
Formate
Co2 and H2O

Question 41

Competitive inhibition binds to

Answer 41

Free enzyme

Question 42

Noncompetitive inhibition binds to

Answer 42

Free enzyme and ES complex

Question 43

Uncompetitive inhibition binds to

Answer 43

ES complex

Question 44

Methanol intoxication causes

Answer 44

Metabolic acidosis

Question 45

Ethylene glycol intoxication causes

Answer 45

Hypocalcemia (stones)
Renal insufficiency
Metabolic acidosis

Question 46

Aldehyde dehydrogenase causes

Answer 46

Small amount of alcohol
Body processes it slowly
Can cause flushing and nausea

Question 47

Treatment for printer fluid suicide
Ataxia, hyperventilation

Answer 47

Increased methanol