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Bio 540 - Biochem > Exam 2 - Intro to Enzymes > Flashcards

Exam 2 - Intro to Enzymes Flashcards

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1
Q

An enzyme that is inactive due to the absence of a cofactor or prosthetic group is a….

A

Apoenzyme

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2
Q

A catalytically active enzyme-cofactor or enzyme-prosthetic group complex is a …..

A

Holoenzyme

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3
Q

A small organic molecule (coenzyme) or metal ion that is required for enzyme activitiy is called a….

A

Cofactor

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4
Q

A cofactor that is covalently associated with an enzyme is a….

A

Prosthetic group

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5
Q

What is the difference between the substrate binding site and the active site?

A
  • Substrate Binding site
    • area of the enzyme that binds specificity with substrate
  • Active Site
    • region of enzyme that caralyzes the reaction
    • Or the specific amino acid residues in the substrate binding site
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6
Q

A control site not within the active or substrate binding site is called the….

A

Allosteric Site

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7
Q

Can an allosteric, effector, molecule increase or decrease the reaction rate?

A
  • It can do both - increase or decrease the reaction…it depends.
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8
Q

What are the 6 classifications of enzymes?

A
  1. Oxidoreductase
  2. Transferase
  3. Hydrolase
  4. Lyase
  5. Isomerase
  6. Ligases
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9
Q

What are our examples of an Oxidoreductase?

A
  • Oxidase and Reductase
    • transfers electrons, usually reversible
  • Dehydrogenase
    • Moves electrons, Look for reducing cofactors like - NAD, NADP, FAD
  • Oxygenase or Hydroxylase
    • Moves Oxygen around
  • Peroxidase
  • Catalase
    • ​Used in reactive oxygen systems
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10
Q

This type of enzyme transfers functional groups to a substrate - 2 substrates = 2 products.

A

Transferase

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11
Q

What are common groups transferred by transferases?

A

Acyl

Amino

Methyl

Glycosyl (sugar)

Phosphate (kinases)

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12
Q

What does a transamerase do? What classification of enzyme would this be?

A
  • Moves Amino acids
  • EC 2
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13
Q
  • This enzyme basically works in the reverse of a condensation reactions, transferring the donor group to water
  • 1 subtrate = [] products
A
  • Hydrolase
  • 2 products
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14
Q

Phosphoprotein phosphatase is a specific enzyme that does what….?

A
  • specific hydrolase that removes phosphate groups.
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15
Q

What are the 7 types of Hydrolases, and what does each do?

A
  1. Esterase - acts on esters
  2. Glycosidase - reverses glycosyl transfers
  3. Peptidase - reverses peptidyltransferase
  4. Thiolase - acts on something attached to acetyl-CoA
  5. Lipase - Acts on phospholipid or fatty acid…BUT not on free cholesterol
  6. Deaminase - Removes a Nitrogen group
  7. Nuclease - Exonuclease (DNAP, RNAse, DNAase)
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16
Q

Lyases

  • EC []
  • Carbon covalently linked to what types of molecules… [] [] [] []
  • May add groups to double []
  • May form double bonds by [] removal
  • May [] or [] water, ammonia, carbon dioxide
  • [] substrate = 2 products
A
  • EC 4
  • N, O, S, P
  • Double Bond
  • Group removal
  • add or remove
  • 1 substrate
17
Q

What are 5 examples of a lyase?

A
  1. Decarboxylase
  2. Synthase (or Lyase….)
  3. Lyase
  4. Aldolase
  5. Hydratase
18
Q
  • This classification of enzyme forms C-C, C-S, C-O, C-N by condensation reactions coupled to ATP cleavage
  • EC []
  • Referred to as []
A
  • Ligases
  • EC 6
  • synthetase
19
Q

What are the 3 examples of Ligases?

A
  • Synthetase
  • Carboyxlase
  • Ligase
    • T4 DNA-ligase
20
Q

Isomerase

  • Transfers groups [] a molecule
  • EC []
  • May alter position of double []
  • May alter position on a [] molecule
  • May alter position of an [] group
  • 1 substrate = [] product
A
  • within
  • EC 5
  • Double bond
  • chiral
  • attached group
  • 1 product
21
Q

This classification of enzyme is also called an “intramolecule lyase”…

A

isomerase

22
Q

What are some examples of isomerases and what do they do?

A
  1. Epimerase
    1. changes connection of molecules on a chiral center when the molecule has >1 chiral centers
  2. Racemase
    1. Changes connection if the molecule only has 1 chiral center
  3. Mutase
    1. Can move around a functional group
23
Q

A reaction order describes how many [] must interact to form products

A

reactants

24
Q

What are the different “ordered” reactions?

A
  • 1st order
  • 2nd order
  • 3rd order, very rare
  • Zero Order
  • Pseudo 1st Order
25
Q

What is unique about zero order and pseudo 1st order reactions?

A
  • Zero Order - only occurs in catalyzed reactions when all active sites are taken (SATURATED)
  • Pseudo 1st Order - two reactants, but one is in such excess that the reaction acts as a 1st order.
26
Q

What 2 terms can be used to describe the rate of the reaction?

A
  • Affinity - Km
  • Velocity - Vmax
27
Q

What are the 3 criteria for Km and Vmax?

A
  1. All substrate goes to SE (substrate-enzyme complex) = substrate saturation
  2. Macimum velocity occurs when you form SE
  3. Saturation is steady state and doesn’t change
28
Q

The [] - [] equation relates the velocity of an enzyme catalyzed reaction to the concentration of substrate?

A

Michaelis-Menten

29
Q

Kcat is….

A
  • number of substrate molecules converted to product molecules by a single molecule of the enzyme in a given unit of time.
30
Q

What are 2 types of cofactors?

A

Coenzyme

Metal ions

31
Q

Coenzymes

  • Small organic molecules that function in [] with an enzyme
  • Can display reaction [] properties with enzymes
  • Example -
A
  • conjunction
  • kinetics
  • NAD (P)
32
Q

Is ATP a coenzyme?

A
  • No - however it can still be an effector molecule
33
Q

NAD (P)

  • Exist in 2 forms - [] and []
  • Common in [] reactions
  • Can work as a [] molecule and typically not a [] group
A
  • Oxdized and reduced
  • dehydrogenase
  • effector, prostethic
34
Q

What are the 3 functions of metal ions?

A
  1. Lewis Acids (bases)
  2. Chelating Agent - binds to other metals and stuff
  3. Helps transfer electrons in redox reaxtions
35
Q

Any reaction that moves electrons requires []

A

Cofactors

36
Q
A

Bio 540 - Biochem (14 decks)

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