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Biochemistry > Lecture 13 & 14 (Exam 2) > Flashcards

Lecture 13 & 14 (Exam 2) Flashcards

1
Q

What are the 3 kinetics trends that are possible?

A

Linear
Hyperbolic
Sigmoidal

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2
Q

Metabolic enzymes are regulated by —

– __________ - different locations

– Enzyme _________ - on/off switch

– Enzyme _________ - volume control

– ________ signals and second messengers - master regulators

A

Compartmentalization
Concentration
Activity
Hormone

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3
Q

The HOW – Basic outcomes

  • ________-level control acts on a single reaction.
  • ________ control targets a different step in the pathway.
A

Substrate

Feedback

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4
Q

The HOW – Basic outcomes

  • Activators (PROMOTE/PREVENT) more products
  • Inhibitors (PROMOTE/PREVENT) more products
A

Promote

Prevent

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5
Q

The WHO – Isozymes

Called _____ and _____ subunits.

A

Mix and match

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6
Q

________ catalyze the same reaction but with different efficiencies. Have different amino acid sequences.

A

Isozymes

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7
Q

The WHAT – Reversible covalent modifications

  • Add 1+ “functional groups” to activate/inactivate the enzyme.
  • Post-translational modifications create _________ amino acids.
A

Nonproteinogenic

***See Lecture 14 Slide 7

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8
Q

What are some common lipid reversible covalent modifications?

A

Myristic acid

Farnesyl

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9
Q

What are common nucleic acid reversible covalent modifications?

A

ADP-ribose

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10
Q

What are common protein reversible covalent modifications?

A

Ubiquitin

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11
Q

In reversible covalent modifications, __________ provide the greatest source of diversity to the proteome.

A

Carbohydrates

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12
Q

Carbohydrates provide many modifications by –

1) ____ vs. ____ linkages
2) Composition of _______
3) Branched vs. Unbranched
4) _______ of oligosaccharide

A

O-
N-
Sugars
Length

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13
Q

This small molecule reversible covalent modification occurs when adding a carboxyl group.

A

y-carboxylation (Carboxyl added to gamma carbon)

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14
Q

This small molecule reversible covalent modification occurs when adding a sulfate group.

A

Sulfation

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15
Q

This small molecule reversible covalent modification occurs when adding an acetyl group.

A

Acetylation

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16
Q

This small molecule reversible covalent modification occurs when adding a phosphate group.

A

Phosphorylation

17
Q

The enzymes catalyzing phosphorylation reactions are called…

A

Protein kinases

18
Q

These are what reverse the effects of kinases by catalyzing the removal of phosphoric groups attached to proteins.

A

Protein phosphatases

19
Q

Note: The name of a kinase indicates on which _____ _____ the phosphate will be added.

A

Amino acid

20
Q

Why is phosphorylation activating?

1) __________: ATP hydrolysis can drive unfavorable reactions (Delta G = -50 kJ/mol)
2) _________: Physiological processes dictate reaction rate
3) Cell processes: ATP amounts dictated by metabolism (energy change) - Signal transduction amplification (catalytic turnover)
4) Shape and charge complementarity: Each phosphate adds (-2) charge and (3+) H-bonds

A

Thermodynamics

Kinetics

21
Q

Why is phosphorylation activating?

1) __________: ATP hydrolysis can drive unfavorable reactions (Delta G = -50 kJ/mol)
2) _________: Physiological processes dictate reaction rate
3) Cell processes: ATP amounts dictated by metabolism (energy change) - Signal transduction amplification (catalytic turnover)
4) Shape and charge complementarity: Each phosphate adds (-2) charge and (3+) H-bonds

A

Thermodynamics

Kinetics

22
Q

The WHERE – Allostery

Allosteric binding does NOT occur at the ______ _____.

A

Active site

23
Q

Homoallostery occurs when the binding of one substrate favors binding of additional substrates, which is called ________.

A

Cooperativity

24
Q

In _________, the kinetics of an enzyme can be controlled by separate substances. (i.e., ACTase with CTP and ATP)

A

Heteroallostery

25
Q

An inhibitor will (INCREASE/DECREASE) the rate of product formation.

A

Decrease

26
Q

An activator will (INCREASE/DECREASE) the rate of product formation.

A

Increase

27
Q

ATCase is (ACTIVATED/INHIBITED) by CTP, and (ACTIVATED/INHIBITED) by ATP.

A

Inhibited

Activated

28
Q

Binding of CTP to ATCase prefers the (T/R) inactive state.

A

T (tense)

29
Q

Binding of ATP to ATCase prefers the (T/R) active state.

A

R (relaxed)

30
Q

The WHEN – Enzyme amount

Protein synthesis regulation = on/off switch

Two levels of control are possible —

1) Transcription regulation at ________
2) Translation regulation at ______

A

Promoters

UTRs (Untranslated regions)

31
Q

Histones control transcription. Histone _________ promotes transcription, while histone _________ prevents transcription.

A

Acetylation

Phosphorylation

32
Q

Histone _________ either promotes OR prevents transcription.

A

Methylation

33
Q

(EUCHROMATIN/HETEROCHROMATIN) is when the DNA is “on” and accessible. Contains acetyl groups/methyls.

A

Euchromatin

34
Q

(EUCHROMATIN/HETEROCHROMATIN) is when the DNA is “off” and compacted. Contains phosphates/methyls.

A

Heterochromatin

35
Q

mRNA levels (DO/DO NOT) correlate to protein levels.

A

Do not

36
Q

miRNAs and UTRs control (TRANSCRIPTION/TRANSLATION).

A

Translation

37
Q

The WHY – Irreversible covalent modification

_________ activation — have to cut/take something away to be active

A

Proteolytic

38
Q

Many important enzymes begin life as _______, which are inactive enzymes.

A

Zymogens

39
Q

Examples of zymogens until proteolytic activation are –

  • Proteases – Digestive enzymes, collagenase (development), and caspases (apoptosis)
  • ________
  • Blood clotting factors
  • ________/hormones
A

Collagen

Insulin

Biochemistry (10 decks)

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