Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

MCM Part 1-First Year > Enzymes And Isoenzymes > Flashcards

Enzymes And Isoenzymes Flashcards

1
Q

What indicates whether the reaction will proceed without the input of energy but are not indicative of the velocity at which the reaction takes place?

A

Numerical values of the standard free energy change

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What enzyme increases the amount of times carbon dioxide and water coverts to bicarbonate and hydrogen?

A

Carbonic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are the most important class of biochemical reactions given that biological oxidation provides most of the energy for aerobic metabolism?

A

Redox reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

When is energy released through the electron transportt chain?

A

When electrons are transferred from fuel molecules through the ETC to oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Energy released in the ETC is used for what?

A

pump hydrogen ions across the mitochondrial membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

How can kidneys regulate the pH of blood?

A

They have the ability to remove protons from the blood in the form of ammonium ion and to reabsorb bicarbonate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What does low pH trigger in the kidney?

A

An increase in both the removal of protons and the reabsorption of bicarbonate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Diabetic ketoacidosis is a condition marked by what?

A

hyperglycemia and low blood pH that often afflicts individuals with uncontrolled diabetes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

The lack of insulin prevents glucose from being taken up by cells to produce energy and consequently, the body switches to degrading _______ for energy.

A

fatty acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

The degradation via beta-oxidation of fatty acids generates acidic compounds called _______.

A

ketone bodies

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are examples of ketone bodies?

A

acetone, acetoacetic acid, beta-hydroxybutyric acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

The dissociation of ketone bodies releases what?

A

H, which causes the pH of blood decrease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What are the symptoms diabetic ketoacidosis?

A

dehydration, vomiting, confusion, and coma and may lead to death

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Describe the gastric proton pump

A

H/K ATPase pump located in parietal cells that line the gastric lumen, pumps protons into gastric lumen, where they combine the Cl to create HCl, a key component of gastic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are drugs that inhibit the gastric proton pump?

A

omeprazole, iansoprazole, esomeprazole.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What does the reduction of HCl production cause?

A

Hypocholorhydria, which leads to a decrease in the absorption of nutrients, an increase in sensitivity to food poisoning, and a reduction in the efficacy of gastric enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is a pharmaceutical agent used for the treatment of chronic gout- a condition caused by the accumulation of uric acid in the synovial fluids surrounding joints and marked by throbbing pain due to the inflammation of joints?

A

allopurinol

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is the target of allopurinol?

A

Xanthine oxidase; converts hypoxanthine to xanthine and then uric acid in purine degradation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Why is allopurinol often described as suicide inhibitor/inactivator?

A

bc its mechanism of action involves binding to the active site of xanthine oxidase, which then converts allopurinol into its active metabolite, alloxanthine. The latter binds tightly to the active site and is only slowly released from it.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

At low concentrations, allopurinol is described as a ________ inhibitor, but at high concentration, it is described as ______ inhibitor?

A

competitive, noncompetitive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What is an autoimmune disease caused by an inhibition of acetylcholine signaling by antibodies that bind to and thus block acetylcholine nicotinic receptors from binding to their cognate ligand, acetylcholine?

A

myasthenia gravis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Patient shows signs of muscle weakness, inability to hold one’s gaze, and fatigue. What is the disease and recommended treatment?

A

Myasthenia gravis

Acetylcholinesterase inhibitors such as physostigmine, neostigmine, and pyridostigmine (reversible inhibitor)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What inhibits metalloenzymes?

A

chelating agents that bind to and remove the metal cofactors from the metalloenzyme. Ethylenediaminetetraacetic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Patient; 8 shows symptoms: abdominal pain, sideroblastic anemia, irritability, headaches, and signs of impaired nervous development and encephalopathy. Patient lives in older building dating back to 1960. Diagnosis

A

Possible lead poisoning. Lead inhibits ALA dehydratase and ferroochelatase, enzymes involved in the biosynthesis ofheme. Treatment with EDTA because lead has an higher affinity for EDTA than does calcium and is excreated in the urine. Children can be treated with chelating agent succimer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What is troponin?

A

a protein complex that plays a role in muscle contraction and relaxation triggered by elevated or depressed levels of intracellular Ca respectively

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What is TN-I?

A

Inhibitory subunit of troponin. cTn-I is found in cardiac muscle. Its serum levels increase after a myocardial infarction

27
Q

In bone disease, higher levels of what enzyme can be expected in the serum?

A

Alkaline phosphatase

28
Q

Obstructive liver disease will cause what enzyme concentrations to be increased in the serum?

A

Sorbitol dehydrogenase

Lactate dehydrogenase

29
Q

If elevated levels of acid phosphatase if found in serum, what diagnosis can be determined?

A

Prostatic cancer

30
Q

Increased levels of amylase in the serum can indicate what disease?

A

Acute pancreatitis

31
Q

increased levels of aldolase and aspartate aminotransferase in the serum can indicate what disease?

A

muscular dystrophy

32
Q

Increased levels of ALT and CK-MM isoform of creatine kinase in the serum can indicate what disease?

A

liver disorder

33
Q

What causes respiratory acidosis?

A

Hypoventilation leads to an increase in the concentration of CO2 in blood. Reaction is shifted to the left which causes an increase in H

34
Q

What causes metabolic acidosis?

A

Addition of a strong acid (lactate, ketone bodies)

Loss of bicarbonate via diarrhea and weakened kidney function

35
Q

What causes respiratory alkalosis?

A

Hyperventilation leads to a decrease in the concentration of CO2 in the blood As a result, the reaction shifts to the right which H decreases

36
Q

What causes metabolic alkalosis?

A

Addition of a strong base like antacid

Loss of acid via vomiting

37
Q

What class of enzymes transfer electrons from a donor to an acceptor? Give an example

A

Oxidoreductases

Dehydrogenases

38
Q

What class of enzymes transfer a functional group between molecules? Give an example

A

transferases

Phosphotransferases

39
Q

What class of enzymes rearrange molecules? Give an example

A

isomerases
Epimerases
Triose phosphate isomerase

40
Q

What class of enzymes add or remove atoms to or from a double bond? Give an example

A

Lyases

C-N-lyases

41
Q

What class of enzymes form bonds with the hydrolysis of ATP?

A

Ligases

42
Q

What class of enzymes cleave bonds via the addition of water? Give an example

A

hydrolases

Esterases, glycosidases, peptidases

43
Q

In peptide hydrolysis, what acts as a general base catalyst and why?

A

The His-57

In the presence of the substrate, His-57 accepts the proton from the Ser-195 hydroxyl group

44
Q

What are small molecules that contribute to the chemical reaction of the enzyme?

A

cofactors

45
Q

Enzyme without its cofactor is called ______.

A

apoenzyme

46
Q

Enzyme bound to cofactor and catalytically active is called _______.

A

haloenzyme

47
Q

Describe metal cofactors

A

Positively charged
Stable coordination of active site groups
Contribute to chemical reactivity

48
Q

What enzyme requires Cu for activity and is part of the ETC?

A

Cytochrome c oxidase

49
Q

What enzyme requires Cu and synthesizes melanin?

A

tyrosinase

50
Q

Fe is a metal ion required for activity of what protein?

A

Heme proteins

51
Q

Name two important enzymes that require Mg for activity

A

ATPase
Adenylate cyclase
Kinases

52
Q

What enzyme detoxifies hydrogen peroxide and uses cofactor Se?

A

glutathione peroxidase

53
Q

Alcohol dehydrogenase, carbonic anhydrase and transcription factors use what cofactor?

A

Zn

54
Q

Small organic molecules often derived from vitamins are called ______ and when bound tightly are called _______.

A

Coenzymes

Prosthetic group

55
Q

Patient symptoms: lesions in corner of mouth and on lips, UV sensitive

A

Ariboflavinosis, coenzyme riboflavin B2 is deficient.
Required for FAD synthesis
Low FAD reduces glutathione reductase activity: cleans up ROS

56
Q

What happens in the active site of alcohol dehydrogenase?

A

NAD+ is reduced to NADH in the conversion of ethanol to acetaladehyde
Cofactors: NAD+ and Zn

57
Q

What catalyzes teh second step of glycolysis?

A

aldolase which is a lyase

F-1,6-BP to DHAP and GAP

58
Q

What acts as a positive effector on pyruvate carboxylase and stimualtes gluconeogenesis?

A

Acetyl CoA

Pyruvate->oxaloacetate

59
Q

What acts as a positive effector on PFK-1 that stimulates glycolysis?

A

Fructose 2,6, BP

60
Q

What acts as a negative effector on PFK-1 that inhibits glycolysis?

A

Citrate

61
Q

What acts as a negative effector on hexokinase that inhibits glycolysis?

A

Glucose 6-P

62
Q

What is the effector outcome of ATP on aspartate carbamoylase?

A

Positive effect that stimulates pyrimidine synthesis

63
Q

What is the effector outcome of CTP on aspartate carbamoylase?

A

Negative effectors that stimulate and inhibit pyrimidine synthesis

64
Q

What are isoenzymes used to diagnose myocardial infarction?

A

LDH-1
CK-MB
Troponin
AST/SGOT1

MCM Part 1-First Year (13 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions