Enzymes Flashcards

1
Q

A common biological reaction without enzyme catalysis will take

A

750,000,000 years

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2
Q

Enzymes are

A

biological catalysts that accelerate the rate of a reaction

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3
Q

Most enzymes are …….

A few enzymes are …….. that are made up of ……….

A

proteins
ribozymes
RNA

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4
Q

Enzymes are not ……….. ………… during the reaction

A

permanently changed

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5
Q

Properties of enzymes

A
  • highly efficient
  • highly specific
  • regulation
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6
Q

Ratio of catalyzed reaction to uncatalyzed reactions

A

kcat/kuncat

for some reactions, this can be up to 10^17

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7
Q

Classes of enzyme specificty

A

absolute
group
linkage
stereochemical

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8
Q

Absolute

A

enzyme reacts with only one substrate

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9
Q

Group

A

enzyme catalyzes reaction involving any molecules with same functional group

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10
Q

Linkage

A

enzyme catalyzes the formation or break up of only certain category or type of bond

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11
Q

stereochemical

A

enzyme recognizes only 1 of 2 enantiomers

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12
Q

How do catalysts work?

A

increase the rate of reactions by lowering the activation energy

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13
Q

Activation Energy

A

the energy required to break bonds

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14
Q

Every enzyme has an

A

active site

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15
Q

Active site

A

pocket or groove on enzyme that binds to substrate

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16
Q

Substrate

A

the reactant on which an enzyme works

17
Q

Mechanism of enzyme action

A

enzyme binds w/ substrate
product is formed at a lower activation energy
product is released

18
Q

Induced fit enzyme model

A

assumes that the enzyme active site is more a flexible pocket whose conformation changes to fit the substrate molecule

19
Q

Lock and key

A

the enzyme is assumed to be the lock and the substrate the key
-the enzyme and substrate are made to fit exactly

20
Q

Why is the lock and key model outdated?

A

the model fails to take into account protein’s conformational changes to fit a substrate molecule

21
Q

Chemical composition of enzymes

A

can either be simple or complex enzymes (holoenzymes)

22
Q

Complex enzymes don’t function without the

A

non-protein part

23
Q

Non-protein part can be

A
  • cofactor
  • coenzyme
  • prosthetic group
24
Q

Inorganic cofactor- minerals

A
  • inorganic

- small

25
Conenzyme-vitamins
- organic | - larger
26
NAD contains the vitamin | FAD contains the vitamin
B3 and B2
27
Both cofactors and coenzymes are not covalently bound to
the enzyme
28
Prosthetic group
tightly bound to the enzyme
29
Enzyme for urea
urease
30
Nomenclature of Enzymes
- in most enzymes names end in -ase - others are named for the substrate and the reaction catalyzed - some are historical-no direct relationship to substrate or reaction type
31
Enzymes are often classified according to the reactions they carry out
``` oxidoreductase transferase hydrolase lyase isomerase ligase ```
32
Oxidoreductase
catalyzes redox reaction | -reductases and oxidases
33
Transferase
transfer a group from 1 molecule to another - transaminases catalyze transfer of an amino group - kinases transfer a phosphate group
34
Hydrolase
break bonds by adding water phosphatases peptidases lipases
35
Lyases
catalyze removal of molecules to form double bonds or the reverse to break double bonds - decarboxylases - synthases
36
Isomerases
catalyze intramolecular rearrangements - epimerases - mutases
37
Ligases
catalyze the joining energy