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Biochemistry > Lecture 10 Enzymes 1 > Flashcards

Lecture 10 Enzymes 1 Flashcards

1
Q

Define oxidoreductases

A

Move electrons: redox reactions

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2
Q

What are the activated carriers in regards to oxidoreductases?

A

NADH
NADPH
FADH2
FMNH2

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3
Q

Define transferases

A

Move a functional group

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4
Q

What are the activated carriers of transferases?

A 
ATP 
pyridoxal phosphate
SAM 
Tetrahydrofolate 
5'-deoxyadenosylcobalamin
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5
Q

Define hydrolyses

A

break a chemical bond by adding water across it

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6
Q

Define isomerases

A

rearrange order of atoms in a molecule (isomerization)

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7
Q

Define lyases

A

Break a chemical bond without using water

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8
Q

Define ligases

A

paste two pieces together (make a chemical bond), uses ATP

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9
Q

Who are the activated carriers for ligase?

A

TPP, coASH, lipoamide, biotin

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10
Q

Describe a nucleophilic substitution

A

swap functional groups

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11
Q

Describe nucleophilic addition

A

add functional groups

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12
Q

Describe carbonyl condensation

A

changes the number of carbons

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13
Q

Describe elimination

A

increases the bond order

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14
Q

Describe oxidation reduction

A

moves electrons: redox. Nicki ford luvs

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15
Q

What are the three types of bonds that take place within substrate binding?

A

Nonpolar van der waals interactions

charge charge interactions

hydrogen bonding interactions

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16
Q

Describe the active site

A
  1. only a few residues out of the protein
  2. 3-D cleft/crevice/pocket, creating a microenvironment (environment will help us do something)
  3. determines substrate specificity by size and charge complementarity
  4. contacts with the substrate through non covalent interactions
17
Q

Describe allosteric binding

A

Does NOT occur at the active site, but follows the same interaction rules as an active site

involves a second substrate which can be an activator or inhibitor

18
Q

Describe competitive binding

A

Something binds to the active site of the molecule

19
Q

Describe allosteric binding

A

Something binds to the molecule at a place that is not the active site

20
Q

Describe competitive inhibition

A

An inhibitor binds to the active site and does not allow substrates to bind

21
Q

Describe allosteric inhibition

A

An inhibitor binds to the molecule and changes the shape of the active site and does not allow the substrates to bind to the molecule

22
Q

Describe allosteric activation

A

The allosteric activator binds to the molecules, changes the shape of the active site that is consistent with what the substrate needs and allows it to bind

23
Q

Define apoenzymes

A

incomplete
inactive
lack cofactor/coenzyme

24
Q

Define holoenzyme

A

whole, active contain a cofactor/coenzyme and require allosteric activation

Biochemistry (12 decks)

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