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Year 1 MCD > Metabolism > Flashcards

Metabolism Flashcards

1
Q

What is the simplest amino acid?

A

Glycine

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2
Q

What bonds combine to stabilise a protein?

A

Disulphide bridges, Hydrogen bonds, Ionic interactions, van der Waal’s, Hydrophobic interactions

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3
Q

In what direction is the polypeptide chain read?

A

From the N terminus to the C terminus

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4
Q

What two patterns can a beta-plated sheet form?

A

Parallel and Anti-parallel

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5
Q

What is the name given to proteins that help other proteins fold?

A

Chaperones

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6
Q

What is the name given to proteins that help other proteins fold?

A

Chaperones

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7
Q

How is glutamate important with regards to blood-clotting?

A

Gultamate is carboxylated to gamma-carboy-glutamate by Vitamin K-dependent carboxylase. The products is important in the blood-clotting cascade.

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8
Q

How does warfarin work?

A

It is an anticoaggulant that inhibits carboxylation of glutamate.

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9
Q

What does glucose-6-phosphatase do?

A

It is a liver enzyme that converts glucose-6p-phosphate into glucose, releasing glucose from stores of glycogen

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10
Q

What does glucose-6-phosphatase do?

A

It is a liver enzyme that converts glucose-6p-phosphate into glucose, releasing glucose from stores of glycogen.

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11
Q

What is Von Gierke’s disease?

A

Deficiency of glucose-6-phosphatase enzyme. Glucose cannot leave the liver. It results in low blood sugar levels, slow growth, hepatomegaly, and short stature.

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12
Q

What are the first two laws of thermodynamics?

A

1st: Energy cannot be created or destroyed
2nd: Entropy can only increase in an isolated system

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13
Q

What is Gibb’s Free Energy equation?

A

(delta)G = (delta)H - T(delta)S

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14
Q

With regards to Gibb’s Free Energy, when does a reaction spontaneously occur?

A

When (delta)G is negative?

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15
Q

What bond is often broken in ATP?

A

The phosphoanhydride bond.

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16
Q

How much energy is released when ATP is broken down into ADP and Pi?

A

-31 KJ/mol

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17
Q

What is the induced fit model?

A

Substate induces a change in conformation of the enzyme, which results in the formation of the active site.

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18
Q

What does lysozyme do?

A

Breaking the peptidoglycan layer of bacterial cell walls. Through hydrolysis of glycosidic bind between N-actetyl glucosamine (NAG) and N-acetyl muramic acid (NAM).

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19
Q

How does lysozyme work?

A

1) Glu35 pronates the oxygen in the glycosidic bond. breaking the bond.
2)

20
Q

How does lysozyme work?

A

1) Glu35 pronates the oxygen in the glycosidic bond. breaking the bond. Asp52 stabilises the positive charge.
2) A water molecule enters and is de-protonated by Glu35, forming a hydroxide ion.
3) The hydroxide ion attacks the remaining sugar molecule adding an OH group.

21
Q

What is the optimum pH of Lysozyme?

A

5.0 where Glu35 is unionised and Asp52 is ionised.

22
Q

Where does glycolysis take place?

A

Cytoplasm

23
Q

What are the first five steps of glycolysis?

A

1) Glucose + ATP -> Glucose-6-phosphate + H+ + ADP. By enzyme hexokinase.
2) Glucose-6-phosphate -> Fructose-6-phosphate. By enzyme phosphoglucose isomerase.
3) Fructose-6-phosphate + ATP -> Fructose-1,6-bisphosphate + ADP + H+. By enzyme phosphofructokinase
4) Fructose-1,6-bisphosphate -> Glyceraldehyde-3-phosphate + Dihydroxyacetone phosphate. By enzyme aldolase.
5) Dihydroxyacetone phosphate -> Glyceraldehyde-3-phosphate. By enzyme triose phosphate isomerase.

24
Q

What are the last five steps of glycolysis?

A

6) 2X Glyceraldehyde-3-phosphate + Pi + NAD+ -> 2X 1,3-bisphosphoglycerate + NADH + H+. By enzyme glyceraldehyde-3-phosphate dehydrogenase.
7) 2X 1,3-bisphosphoglycerate +ADP -> 2X 3-phosphoglycerate + ATP. By enzyme phosphoglycerate kinase
8) 2X 3-phosphoglycerate -> 2X 2-phosphoglycerate. By enzyme phosphoglycerate mutase.
9) 2X 2-phosphoglycerate -> 2X Phosphoenolpyruvate + H20. By enzyme enolase.
10) 2X Phosphoenolpyruvate + ADP -> 2 X Pyruvate + ATP. By Pyruvate kinase.

25
Q

What are the last five steps of glycolysis?

A

6) 2X Glyceraldehyde-3-phosphate + Pi + NAD+ -> 2X 1,3-bisphosphoglycerate + NADH + H+. By enzyme glyceraldehyde-3-phosphate dehydrogenase.
7) 2X 1,3-bisphosphoglycerate +ADP -> 2X 3-phosphoglycerate + ATP. By enzyme phosphoglycerate kinase
8) 2X 3-phosphoglycerate -> 2X 2-phosphoglycerate. By enzyme phosphoglycerate mutase.
9) 2X 2-phosphoglycerate -> 2X Phosphoenolpyruvate + H20. By enzyme enolase.
10) 2X Phosphoenolpyruvate + ADP -> 2 X Pyruvate + ATP. By Pyruvate kinase.

26
Q

What is the difference between substrate level phosphorylation and oxidative phosphorylation?

A

Substrate level phosphorylation is the production of ATP by direct transfer of a high energy phosphate group. Oxidative phosphorylation is where ATP is produced using energy derived from electrons in an electron transport system.

27
Q

What are the three possible fates of pyruvate?

A

1) Converted into lactate
2) Converted into ethanol
3) Converted into Acetyl-CoA

28
Q

How is pyruvate converted into lactate?

A

Pyruvate + NADH + H+ -> Lactate + NAD+. By enzyme Lactate dehydrogenase.

29
Q

How is pyruvate converted into ethanol?

A

1) Pyruvate + H+ -> acetaldehyde + CO2. By enzyme pyruvate decarboxylase.
2) Acetaldehyde + NADH + H+ -> Ethanol + NAD+. By enzyme alcohol dehydrogenase.

30
Q

How is pyruvate converted into ethanol?

A

1) Pyruvate + H+ -> acetaldehyde + CO2. By enzyme pyruvate decarboxylase.
2) Acetaldehyde + NADH + H+ -> Ethanol + NAD+. By enzyme alcohol dehydrogenase.

31
Q

What clinical significance does LDH (Lactate Dehydrogenase) have?

A

Elevated LDH levels can point to ischaemia, hepatitis, muscle injury, muscular dystrophy.

32
Q

What does creatine kinase do?

A

Enzyme that catalyses the reaction:

Creatine phosphate + ADP -> Creatine + ATP

33
Q

Where is pyruvate converted into acetyl-CoA?

A

In the mitochondria.

34
Q

How is pyruvate converted into Acetyl-CoA?

A

Through the pyruvate dehydrogenase complex which catalyses:

Pyruvate + NAD+ +CoA -> Acteyl-CoA + CO2 + NADH + H+

35
Q

What are the components of the pyruvate dehydrogenase complex?

A

Pyruvate decarboxylase with Thymine Pyrophosphate (TPP) prosthetic group.
Lipoamide reductase-transacetylase with Lipoamide prosthetic group.
Dihydrolipoyl dehydrogenase with FAD prosthetic group.
NAD+ and CoA co-factors.

36
Q

How does the pyruvate dehydrogenase complex produce Acetyl-CoA?

A

Pyruvate

37
Q

How does the pyruvate dehydrogenase complex produce Acetyl-CoA?

A

1) Pyruvate is decarboxylated with TPP forming Hydroxyethyl-TPP by enzyme Pyruvate Decarboxylase.
2) Hydroxyethyl-TPP is oxidised and transferred to Lipoamide (which replaces TPP) to become acetylipoamide. Catalysed by lipide reductase transacetylase.
3) Transfer of acetyl group to CoA to give actyl-coA, leaving a reduced lipoamide.

38
Q

Why can acetyl CoA readily donate acetate to other molecules?

A

Thioester bond is highly energetic and is readily hydrolysed.

39
Q

What are the first four steps in the TCA cycle?

A

1) Oxaloacetate + Acetyl-CoA -> Citrate + HS-CoA. By enzyme Citrate synthase.
2) Citrate -> Isocitrate. By enzyme aconitase.
3) Isocitrate + NAD+ -> (alpha)-ketogluterate + CO2 + NADH + H+. By enzyme isocitrate dehydrogenase
4) (alpha)-ketogluterate + HS-CoA + NAD+ -> Succinyl-CoA + CO2 + NADH + H+. By enzyme (alpha)-ketogluterate dehydrogenase complex.

40
Q

What are the last four steps in the TCA cycle?

A

5) Succinyl-CoA + GDP + Pi -> Succinate + GTP + HS-CoA. By enzyme Succinyl-CoA synthetase.
6) Succinate + FAD -> Fumerate + FADH2. By enzyme succinate dehydrogenase.
7) Fumarate + H20 -> Malate. By enzyme fumarase.
8) Malate + NAD+ -> Oxaloacetate + NADH + H+. By malate dehydrogenase.

41
Q

What does one turn of the TCA cycle produce?

A

2X CO2
3X NADH
1X FADH
1X GTP

42
Q

Where does the Krebs Cycle take place?

A

The enzymes are in the mitochondrial matrix except for succinate dehydrogenase which is part of Cytochrome B-C1 complex.

43
Q

Why can the Krebs Cycle only take place in aerobic conditions?

A

FADH2 and NADH need O2 to be re-oxidised.

44
Q

Why can the Krebs Cycle only take place in aerobic conditions?

A

FADH2 and NADH need O2 to be re-oxidised.

45
Q

How much ATP is produced per molecule of NADH and FADH2

A

NADH: 3 ATP
FADH: 2 ATP

46
Q

How many ATP molecules is produced from one glucose molecule?

A

38

47
Q

How are amino acids degraded?

A

Remove the main group (eventually excreted as urea) whilst the carbon skeleton is fed into the Krebs cycle or production of glucose.

Year 1 MCD (8 decks)

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