Biochem 4

Front 1

Enzyme nomenclature

Back 1

Common name and 4 digit code

First number major class. remaining 3 are subclasses

Front 2

Acid base catalysis

Back 2

Acid-donation or release of proton lowers free energy of transition states

Base-acceptance of a proton/removal from reactant lowers transition state free energy

-some reactions undergo both at the same time

Hint 2

Front 3

Covalent catalysis

Back 3

-accelerates reaction through formation of catalyst substrate bond. Also known as nucleophilic catalysis. Bonds transform

Hint 3

Front 4

Metal ion catalysis

Back 4

Enzymes requiring metal ion cofactor for activity.

Common fe2+,fe3+, cu2+, mn 2+, co2+, zn+

Hint 4

Front 5

Proximity and orientation effects

Back 5

Proximity and orientation of substrates/reagents can enhance rate

Hint 5

Front 6

Preferential binding of transition state

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Enzyme may bind to transition state with higher affinity than to substrates or reactants. By doing so,increases concentration of transition state and therefore reaction

Front 7

Enzyme specificity

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-stereospecific, geometric, physical.

-enzymes are chiral and have chiral active sites making them very stereospecific in their reactions

Front 8

Protein nature of enzymes

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-enzymes are made of amino acids just like proteins.

-because there are only 20 amino acids, this limits the variety of enzymes which can require them to have cofactors, coenzymes, prosthetic groups

Front 9

Cofactors

Back 9

Can be metal cation,small organic molecules or anything enzyme needs to carry out catalysis of a reaction

Front 10

Coenzymes

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Cofactors that are small organic molecules termed coenzymes. If they are tansiently associated with an enzyme,also called cosubstrate

Front 11

Prosthetic group.

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Coenzyme permanently associated with enzyme. Can be non covalent or covalently bound

Front 12

Holoenzymes

Back 12

Enzyme with cofactors bound to active site. Can conduct cataly

Front 13

Apoenzyme.

Back 13

Enzyme that are not bound to their cofactor and are inactive

Front 14

Transition state analogs

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-chemical compounds with similar chemical structure to the transition state

-act as competitive inhibitors by blocking the enzyme active state

Front 15

Zymogens

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Inactive precursors of enzymes

Front 16

Serine proteases

Back 16

Catalyze peptide bonds through several forms of catalysis. Acid base,transition state, covalent bond, proximity and orientation

Front 17

General serine protease stuff

Back 17

Named so because of common mechanism involving reactive site serine residue

Participates in digestion, inflammation, blood clotting and other processes

Front 18

DIPF and serine protease

Back 18

DIDF and similar compounds react with active site irreversibly inhibiting serine proteases

Front 19

Specificity pockets of serine proteases

Back 19

Side chains of key residues determine the size and nature of the specificity pocket

Hint 19

Front 20

Active site residue in serine proteases

Back 20

Trypsin, chymotrypsion and elastase have very similar primary sequence. Some bear no discernable similarities but still contain same active site and similar catalytic abilities

Hint 20

Front 21

Serine mechanism step 1

Back 21

Back (Definition)

Front 22

Serine protease mech step 2

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Back (Definition)

Front 23

Serine mech step 3

Back 23

Back (Definition)

Front 24

Serine mech step 4

Back 24

Back (Definition)

Front 25

Serine mech step 5

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Back (Definition)

Front 26

Competitive inhibition

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Increases km app

Front 27

Uncompetitive

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Decreases km and vmax app

Front 28

Mixed (non competitive)

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Decreases vmax app, may increase or decrease km app

Front 29

Mixed/non competitive ihabiton reaction diagram

Back 29

Back (Definition)

Front 30

Mixed/non competitive graph

Back 30

Back (Definition)

Front 31

Uncompetitive inhibition reaction diagram

Back 31

Back (Definition)

Front 32

Uncompetitive inhabiting graph

Back 32

Back (Definition)

Front 33

Competitive inhabiting graph

Back 33

Back (Definition)

Front 34

Competitive inhibition enzyme graph

Back 34

Back (Definition)

Front 35

What is turnover rate equal to

Back 35

Back (Definition)

Front 36

What best describes catalytic efficiency

Back 36

Back (Definition)

Front 37

What is km describes an ideal enzyme

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Small km

Front 38

What kcat means an ideal enzyme

Back 38

Larger kcat means more ideal enzyme