Topic 4 (enzymes Intro) Flashcards

1
Q

Zn(2+) can be found in which enzyme?

What does it do

A

Carbonic Anhydrase

Activates it for reaction with CO2

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2
Q

Mg(2+) can be found in what type of enzymes

A

Kinases

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3
Q

Ca(2+) can be found as a regulatory enzyme. What enzyme?

A

Calpain

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4
Q

Riboflavin (B2) coenzyme and deficiency disease

A

FAD/FMN

Ariboflavinosis

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5
Q

Niacin conenzyme and Deficiency disease

A

NAD+/NADP+

Pellagra

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6
Q

Thaiamine (B1) enzyme and deficiency

A

Thiamine Pyrophosphate

Beriberi

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7
Q

Vit C enzyme and deficiency

A

Hydroxylases

Scurvy

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8
Q

Folic Acid enzyme and deficiency

A

Tetrahydrofolate

Folate Def.anaemia

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9
Q

Pyridoxal (B6) enzyme and deficiency

A

Microcytic anaemia

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10
Q

G6PDH is caused by what?

Function?

A

X-linked recessive mutation

Produces NADHP biosynthesis for nucleic acids/lipids

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11
Q

Symptoms of G6PDH (2)

A

Haemolytic crisis

Jaundice

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12
Q

What can trigger G6PDH

A

Foods / infection / drugs

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13
Q

30% glucose oxidation goes through what?

A

Pentose Phosphate Pathway in Liver

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14
Q

High …. activates G6PDH

A

NADP+

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15
Q

What type of anaemia can arrise from G6PDH deficiency

A

Primaquine-induced haemolytic anaemia

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16
Q

Thiopurine Methyl Transferase (NOT FINISHED CARD)

A

NOT FINISHED

17
Q

What is A1-antitrypsin role

A

Prevents proteases attacking tissue

18
Q

What is pancreatic trypsin inhibitor role

A

Controls activity of digestive enzyme

19
Q

Antithrombin 3 role

A

Switches off blood clotting system

20
Q

A1-antitrypsin // Antithrombin 3 // pancreatic trypsin inhibitor are all what type of proteases?

A

Serine Protease Inhibitors

21
Q

What type of enzyme phosphorylate other enzymes

A

Protein Kinases

22
Q

Where is the phosphate taking from in phosphorylation

A

Y-Phosphate from ATP

23
Q

What is a zymogen?

A

Inactivated proteolytic enzyme

24
Q

How is a zymogen activated?

A

Irreversible removal of part of peptide chain

25
Q

Why does cleaving of peptide chain in zymogens done?

A

Prevent premature activation of enzymes in wrong place/ time

26
Q

What type of protein is chymotrypsin?

A

Serine Protease

27
Q

Structure of chymotrypsin

A

3 polypeptide chain - linked by disulphide chains

28
Q

name the 3 stages of a fully active chymotrypsin

A

Zymogen (polypeptide chain)

(pi)-chymotrypsin (via trypsin)

a-chymotrypsin (via chymotr)

29
Q

What is the catalytic triad found in chymotrypsin

A

Aspartate

Histidine

Serine

30
Q

How is Trypsinogen activated to become Trypsin + Enzyme

A

Removal of AA 1-6

Via enteropeptidase

31
Q

What does Trypsin convert?

A

Procarboxypeptidase -> Carboxypeptidase

32
Q

What does TPA convert?

A

Plasminogen –> Plasmin

33
Q

Name a recombinant TPA

A

Alteplase