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Pass Program > Chapter 5: Enzymes > Flashcards

Chapter 5: Enzymes Flashcards

1
Q

What proteins speed reactions up?

A

enzymes

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2
Q

In competitive inhibition where do the substrate and inhibitor bind

A

same site, active site; Vmax stays the same

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3
Q

In noncompetitive inhibition where do the inhibitors bind?

A

allosteric site (different site); may cause a change in active site and therefore, substrate cannot bind so Vmax decreases

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4
Q

Why do we prefer competitive inhibitors to non-competitive inhibitors?

A

They are reversible.

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5
Q

Wen you give electrons away it is called ____

A

oxidation

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6
Q

When you accept electrons it is called

A

reduction (OIL RIG) oxidation is loss, reduction is gain

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7
Q

What is oxidative phosphorylation?

A

When NADH, FADH2, and electrons are made into ATP (energy)

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8
Q

Where does the NADH come from in the oxidative phosphorylation?

A

from pyruvate dehydrogenase, and 3 enzymes in citrate cycle : isocitrate dehydrogenase, alpha-ketoglucarate dehydrogenase, and malate dehydrogenase

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9
Q

Where does FADH2 come from in oxidative phosphorylation?

A

succinate dehydrogenase

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10
Q

What coenzyme is needed at the II of ETC?

A

coenzyme Q

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11
Q

What is an electron carrier from III to IV in ETC?

A

cytochrome C

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12
Q

What is a coenzyme of Complex IV?

A

Copper

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13
Q

What occurs at Complex V?

A

phosphorylation (ADP—ATP)

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14
Q

What common drug for cholesterol destroys Coenzyme Q and Cytochrome C?

A

statins

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15
Q

What drug can block Complex 1?

A

Rotenone (pesticide)

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16
Q

What drug can block Complex IV?

A

CO, CN, Chloramphenicol

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17
Q

Why will the Hb saturation be normal in carbon monoxide poisoning?

A

Because CO is a competitive inhibitor of O2; that is why to overcome CO we must give 100% O2 (increase substrate, up Km).

18
Q

What kinds of bacteria does chloramphenicol cover? Why don’t we like to use it?

A

all gram +, simple gram -, rickettsia; affects all rapidly dividing cells by blocking the 50s subunit and its peptidyl transferase; causes aplastic anemia and gray baby syndrome

19
Q

Compounds that grab protons in ETC and drag them back into the matrix and stops ATP synthesis, releasing a lot of energy are called __________.

A

uncouplers

20
Q

Examples of uncouplers

A

aspirin, succinylcholine (malignant hyperthermia), haloperidol (neuroleptic malignant syndrome), DNP (dinitrophenol) pesticide, free fatty acids

21
Q

Tx for malignant hyperthermia and neuroleptic malignant syndrome?

A

dantrolene: stabilizes sarcoreticular and ryandine arm so no Ca for contraction

22
Q

What does uncoupling do to the liver?

A

shrinks it

23
Q

What conditions cause microsteatosis of liver?

A

pregnancy, tylenol poisoning, Reye’s syndrome

24
Q

What conditions cause macrosteatosis of liver?

A

obesity (NAFLD); and alcohol

25
Q

What kind of enzyme phosphorylates a stubstrate using ATP?

A

kinase

26
Q

What is a cofactor for kinase?

A

magnesium

27
Q

What kind of enzyme phosphorylates a substrate using free phosphate?

A

phosphorylase

28
Q

What kind of enzyme creates an isomer from a substrate?

A

isomerase

29
Q

What has the same chemical makeup and structure but differ around one chiral carbon?

A

epimer

30
Q

What kind of enzyme makes epimers?

A

epimerase

31
Q

What kind of enzyme moves a side chain from one carbon to another carbon?

A

mutase

32
Q

What kind of enzyme transfers a side chain from one substrate to another?

A

transferase

33
Q

What kind of enzyme transfers amino acids from or onto amino acids?

A

transaminase

34
Q

What kind of enzyme cuts carbon-carbon bonds and must use ATP to do it?

A

lyase

35
Q

What kind of enzyme uses carbon dioxide to create a carbon-carbon bond but uses biotin as a cofactor?

A

carboxylase

36
Q

What kind of enzyme is used to stack substrates together to create a product?

A

synthase

37
Q

What kind of enzyme uses ATP to stack substrates together to create a new product?

A

synthetase

38
Q

What kind of enzyme uses a cofactor to take hydrogens off substrates?

A

dehydrogenase

39
Q

What kind of enzyme uses water to break bonds?

A

hydrolase

40
Q

When a sulfur bond is broken in the reaction, what word do we add in front of enzyme name?

A

Thio–

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