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PHARM 113 > ENZYMES PART 1 > Flashcards

ENZYMES PART 1 Flashcards

1
Q

Dehydrogenase

A

Removes hydrogen
Two way function, can catalyze backward reaction

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2
Q

Major Classes of Enzymes

A

EC 1: Oxidoreductase
EC 2: Transferase
EC 3: Hydrolases
EC 4: Lyases
EC 5: Isomerases
EC 6: Ligases
EC 7: Translocases

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3
Q

Reaction rate

A

Higher

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4
Q

Reaction condition

A

Mild

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5
Q

Reaction specificity

A

Specific

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6
Q

Activity regulation

A

Regulated under normal condition

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7
Q

Systematic Name

A

Substrate:Cosubstrate Major Class

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8
Q

EC1: Oxidoreductase

A

Redox reaction
Elimination reaction

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9
Q

EC2: Transferases

A

Transfer of groups
Substitution reaction

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10
Q

EC3: Hydrolase

A

Hydrolysis
Uses H2O to break covalent bonds

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11
Q

EC4: Lyases

A

Covalent bond breaking
Produces double bond (e.g. o==o)

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12
Q

EC5: Isomerases

A

Isomers
Exchange of functional groups

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13
Q

EC6: Ligases

A

Formation of new covalent bond
ATP as an activtor of the substrate
Convert poor leaving group into a good leaving group

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14
Q

Synthase

A

No ATP

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15
Q

Synthetase

A

Uses ATP

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16
Q

EC7: Translocases

A

Extracellular to intracellular
Uses ATP for conformation changes

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17
Q

Isozymes

A

Enzymes with quaternary structure
Combination of subunits differs in different tissues
Useful in diagnosing sites of tissue, injury, cell death

18
Q

Enzymes that have same substrate, classification, reaction but with different amino acid residues and specificity and regulation

A

Isozymes

19
Q

Isomer enzymes

A

Isozymes

20
Q

Structures of enzyme

A

Active site
Binding site
Catalytic site
Substrate
Cosubstrate

21
Q

Binding site

A

Where substrate and cosubstrates bind

22
Q

Catalytic site

A

Near the binding site
Where catalysis happens

23
Q

Important binding interactions

A

H bond
Ionic bond
Hydrophobic interactions

24
Q

Transition state

A

Bonds are in the process of being formed and broken
Structure resembles that of the unstable intermediate
Not likely to be as characterized as those of its reaction occuring

25
Q

More theoretical, unstable
Cannot be isolated

A

Transition state

26
Q

Unstable intermediate

A

A chemical species with just formed bonds
Exists at lower energy possibly between the energy peaks of 2 transition states

27
Q

Could be isolated or chemically trapped (usuallt at lower temp)

A

Unstable intermediate

28
Q

Substrate binding

A

Lock and key
Induced fit model

29
Q

Specificity of activity

A

Reaction specificity
Absolute specificity
Group specificity
Linkage specificity
Optical specificity
Geometric specificity

30
Q

Reaction specificity

A

For specific reaction
Ex. Oxidoreductase for redox reaction not for phosphorilization

31
Q

Absolute specificity

A

For specific substrate
Ex. Glucokinase for glucose but not for other hexose

32
Q

Group specificity

A

Target specific functional group
Ex. Hexokinase for any hexose

33
Q

Linkage specificity

A

For specific linkage
Ex. Amidase hydrolyze amide linkages but not ester

34
Q

Optical (stereo) specificity

A

For specific D/L configuration
Ex. L-aminoacyl esterase catalyzes the reaction of L-amino acyl but not D-amino acyl

35
Q

Geometric specificity

A

For specific shape/geometry
Ex. Aromatic acyl aminoesterase for aromatic compounds

36
Q

Cofactors

A

Metal ions
Prosthetics
Coenzymes

37
Q

Metalloenzymes

A

Tightly bound
Transition metals: Fe2+ Fe3+ Cu2+ Zn2+

38
Q

Metal enzymes

A

Losely bound
Alkali and akaline earth metals: K Na Ca Mg

39
Q

Prosthetics Group

A

Non amino acid residues

Covanlently bound to the enzyme
Dialyzable
Thermostatble

40
Q

Coenzymes

A

Non protein organic molecules
Transiently associated
Redox and transfer reactions
Precursor: vitamins

41
Q

Holoenzyme

A

Fully functional form of the enzyme
Apoenzyme and cofactor

42
Q

Apoenzyme

A

Protein only w/o cofactor
Inactive
Nonfunctional

PHARM 113 (5 decks)

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