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MCAT ALL > Enzymes > Flashcards

Enzymes Flashcards

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MCAT flashcards
1
Q

Covalent catalysis

A

Enzyme temporally covalently bonds to the substrates and acts as “electron sink” or “carrier”; it carries the electron for a moment

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2
Q

Acid Base Catalysis

A

Move H+ electron

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3
Q

Spacial Enzyme

A

Increases the likely hood of successful collisions

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4
Q

Electrostatic

A

Use metal or charged ions that helps stabilize some other species

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5
Q

Substrate

A

Molecule upon which an enzyme acts

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6
Q

Active site

A

Location within enzyme where substrate is held during chemical reaction; site of catalysis

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7
Q

Lock and key theory

A

Enzyme active site (lock) already in appropriate confirmation for substrate( key) to bind. Enzyme and substrate complementary
no alterations in 3D or 4D confirmation

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8
Q

Induced fit

A

Enzyme and substrate go conformational changes to interact fully
Substrate changes to fit the shape of the enzyme

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9
Q

Apoenzyme

A

Enzymes without cofactors

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10
Q

Haloenzymes

A

(have)

Enzymes that have cofactors

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11
Q

Fat soluble vitamins

A

DAKE

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12
Q

Cofactors

A

Inorganic molecules or metal ions
- ingested as dietary minerals
Ex: DNA polymerase uses Mg2+ as cofactor

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13
Q

Coenzymes

A

Small organic groups or carriers

vitamins such as NAD+ or FAd, CoenzymeA

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14
Q

At saturation

A

Enzyme working at its maximum velocity called vmax

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15
Q

What is the only way to increase vmax

A

increase enzyme concentration

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16
Q

Rate of reaction (V)=

A

Vmax [S]/ (km + [S])

17
Q

km=

A

the substrate concentration were Vo = 1/2 Vmax

lower km= better enzyme working

18
Q

Kcat

A

Turnover number

How many substrates an enzyme can turn into products in 1 sec at max speed

19
Q

Cooperativity

A

Have a sigmoidal curve
-Have multiple subunits and multiple binding sites
-Binding to one site increases the binding to other to other subunits
Example: Hemoglobin

20
Q

Positive cooperativity

A

Substrate binding increases affinity for subsequent substrate (hemoglobin)

21
Q

Negative Cooperativity

A

Negative-cooperatively - Substrate binding decreases affinity for subsequent substrates

22
Q

Optimal Blood pH

A

7.4

23
Q

Pepsin in stomach pH

A

2

24
Q

Pancreatic enzyme in small intestine pH

A

8.5

25
Q

Salinity

A

Salt concentration increasing= disrupt hydrogen and ionic bonds, causing changes in confirmation of the enzyme and even denaturization

26
Q

Ideal body temp

A

37C, 98.6F, 310K

27
Q

Competitive Inhibitor

A

Binding Site: Active Site
Impact on Km: Increases
Impact on Vmax: not changed
-increasing substrate concentration to overcome

28
Q

Non-competitive

A

Binding Site:Allosteric Site causing confirmation changes in the enzyme
Impact on Km: Unchanged
Impact on Vmax: Decreases

29
Q

Mixed

A

Binding Site:Allosteric Site or ES complex
Impact on Km: Increases or decreases
Impact on Vmax: Decreases

30
Q

Umcompetitive

A

Binding Site:Allosteric Site only to ES complex and locks the substrate in the enzyme preventing its release
Impact on Km: Decrease
Impact on Vmax: Decreases

31
Q

Regulated Enzyme

A

Allosteric Enzyme
Covalent (reversible)
Enzyme itself
“ACE”

32
Q

Allosteric Enzyme

A

Regulator binds to the non-active site, and it activates/inactivates/inhibits the enzyme
-multiple binding sites

33
Q

Covalent (reversible) Modified enzymes

A

Enzymes can be activated by phosphorylation or dephosphoralation
- ex :Glycosylation mainly refers in particular to the enzymatic process that attaches glycans to proteins,

34
Q

Enzyme itself

A

Zymogens: are secreted in inactive form and are activated by cleavage (because they are dangerous if not controlled)

  • irreversibly activated
  • have an “-ogen” ending
    ex: pepsinogen

MCAT ALL (56 decks)

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