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BMS 100 > Proteins and Enzymes > Flashcards

Proteins and Enzymes Flashcards

1
Q

bond that occurs between two oppositely charged amino acids

A

salt bridge

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2
Q

which bond helps protect a protein from denaturation during changes in blood pH or salt concentrations?

A

disulfide bonds - strong bonds

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3
Q

what is an example of an extracellular protein that is held together by disulphide bonds?

A

insulin

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4
Q

a protein composed of two subunits

A

dimer

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5
Q

a protein composed of several subunits

A

oligomer

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6
Q

a protein composed of many subunits is called a

A

multimer

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7
Q

what are proteins that help other proteins get into their correct shape and correct cellular locations?

A

chaperones

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8
Q

how are chaperone proteins released?

A

ATP hydrolysis

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9
Q

___ are common chaperone proteins that bind and stabilize portions of proteins not yet folded

A

heat shock proteins

  • get induced in cells during various stress conditions produced by cellular insult, environmental changes, temperature, infections, tumors etc
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10
Q

a ___ is any repeating structural unit within a multimeric protein

A

protomer

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11
Q

enzymes are an example of a type of ____ protein

A

globular

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12
Q

enzymes are protein ____ that speed up specific reactions and remain ______ by the reaction

A

protein catalysts that speed up specific reactions and remain unchanged by the reaction

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13
Q

the minimal amount of energy needed to make/break the bonds necessary for a reaction to occur

A

activation energy

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14
Q

Enzyme molecules contain a special cleft called the

A

active site

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15
Q

The active site forms by precise _____ structure of the protein

A

quaternary

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16
Q

Amino acids in the active site participate in substrate binding and catalysis

A
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17
Q

Binding of substrate is thought to induce a conformational change in shape of the enzyme is called

A

the Induced fit model

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18
Q

the addition or removal of a proton can make a substrate more reactive

A

acid-base effect

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19
Q

Which amino acid side chain do you think can function easily as an acid or a base?

A

positively or negatively charged amino acids

20
Q

A nucleophilic side group in the enzyme active site forms a temporary covalent bond with the substrate

A

Covalent catalysis

21
Q

Common nucleophilic side groups include:

A
  • Asp and Glu (R-COO-)
  • Ser (R-OH) and Cys (R-SH)

Serine and Cystein are only weakly nucleophilic, but their nucleophilicity is enhanced by the presence of other amino acids that can remove the H

22
Q

molecules that aid in substrate recruitment

A

cofactors and coenzymes

23
Q

Cofactors are typically metal cations

A

Mg and Zn

24
Q

We have already discussed the role of Mg2+ in several glycolytic enzymes involving ATP. What was the role of magnesium?

A
  • Magnesium helped to position the ATP in the enzyme active site
  • Helped to stabilize the negative changes on the ATP
25
Q

examples of coenzymes?

A

Typically derived from vitamins

B3: NAD+ <>NADH + H+

Can accept or donate elections in redox reactions

26
Q

3 ways coenzymes and cofactors can help enzymes speed up reactions

A
  1. help position the substrate in the active site
  2. stabilize negative charges on the substrate or the TS to make it easier for a nucleophilic attack to occur
  3. can accept/donate electrons in redox reactions
27
Q

what is the optimal temperature for enzymes

A

the temperature of the organism

28
Q

Do you think a fevers are good or bad?

A

There are benefits to a certain point

  • Enzyme activity can be increased, metabolism can be increased (to fight infection) and bacteria can no longer function

BUT temps that are too high can cause enzymes to not function = fatality

29
Q

Changing the pH can change the ______ state of the enzyme and/or the substrate

A

protonation

30
Q

What types of bonds between Enzyme and Substrate would potentially be disrupted by a change in pH?

A

H-bonds – for example:
- If an H is removed, no H-bond can be formed
- If an H is added, an H-bond might form that is not usually formed.

Electrostatic interactions - for example:
- Adding an H can turn COO- into COOH
- Removing an H can turn NH3+ into NH2

31
Q

Main site of intracellular enzymatic degradation for a wide range of molecules. They have proteolytic enzymes that break unwanted material in the cell.

A

function of lysosome

32
Q

enzymes can be controlled in four main ways

A
  1. genetic
  2. covalent modification
  3. allosteric regulation
  4. compartmentalization
33
Q

Enzymes transcription can be induced or repressed
based on the needs of the cell

A

genetic modification

34
Q

Involves altering the structure of an enzyme (or “proenzyme”) by making or breaking covalent bonds

A

covalent modification

35
Q

Involves the addition or removal of a group to the enzyme that causes it to convert to its active or inactive form

A

reversible covalent modifcation

36
Q
  • Other common groups that can be added to or removed
    enzymes include ____ and ______ groups
A

methyl and acetyl

37
Q

The main regulated enzyme in glycogenesis is ________ by phosphorylation

A

deactivated

38
Q

while the main enzyme in
glycogenolysis is _______ by phosphorylation.

A

activated

39
Q

what enzyme in glycogenolysis is activated by phosphorylation

A

Glycogen phosphorylase kinase
and Glycogen phosphorylase

40
Q

what enzyme in glycogenesis is deactivated by phosphorylation

A

glycogen synthase

41
Q

Involves cleavage of peptide
bonds in proenzymes or zymogens. Make sure the enzyme is not used until it is in the correct location and until it is needed.

A

Irreversible covalent
modification

42
Q

Binding to enzyme’s allosteric site changes the conformation and activity of the enzyme. Changes the binding affinity of the substrate at the active site

A

Allosteric modification

43
Q

Increase binding of the substrate to the enzyme

A

Effector = activator

44
Q

Decrease binding of the substrate to the enzyme

A

Effector = inhibitor

45
Q

Separation of enzymes from opposing pathways into different cellular compartments, and selective transportation of substrates

A
  1. Compartmentalization
46
Q

Creation of unique microenvironments

A

2.Compartmentalization

BMS 100 (37 decks)

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