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BioChem 1st Shifting > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Enzymes are predominantly protein in nature with the exception of _____

A

ribozymes

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2
Q

Enzymes increase the rate of a reaction by ___ to ___

A

10^9 - 10^20

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3
Q

Protein part of an enzyme

A

Apoenzyme

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4
Q

Non-protein portion of an enzyme that is necessary for catalytic function

A

Cofactor

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5
Q

Examples of cofactor (2)

A

Zn2+ and Mg2+

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6
Q

Non-protein organic molecule, frequently a B vitamin, that acts as a cofactor

A

Coenzyme

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7
Q

Compound/s whose reaction an enzyme catalyzes

A

Substrate

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8
Q

Specific portion of the enzyme to which a substrate binds during reaction

A

Active site

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9
Q

Any process that initiates or increases the activity of an enzyme

A

Activation

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10
Q

Portion on the enzyme surface where inhibitors/activators bind to regular catalytic reactions

A

Allosteric site

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11
Q

Compounds that slows down the rate of the reaction

A

Inhibitor

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12
Q

Process that makes an active enzyme less active or inactive

A

Inhibition

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13
Q

_____ catalyzes the hydrolysis of peptide bonds formed by the carboxyl group of lysine and arginine

A

Trypsin

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14
Q

Effect of enzyme in the activation energy

A

Lower activation energy

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15
Q

A rigid three-dimensional body where the enzyme surface contains the active site

A

Lock-and-key model

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16
Q

The active site becomes modified to accommodate the substrate

A

Induced-fit model

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17
Q

Classification of enzyme: oxidation-reduction reaction

A

Oxidoreductases

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18
Q

Classification of enzyme: group transfer reactions

A

Transferases

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19
Q

Classification of enzyme: hydrolysis reactions

A

Hydrolases

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20
Q

Classification of enzyme: Addition of two groups to a C-C double bond, or removal of two groups to create a C-C double bone

A

Lyases

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21
Q

Classification of enzyme: isomerization reactions

A

Isomerases

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22
Q

Classification of enzyme: joining to two molecules

A

Ligases

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23
Q

Classification of enzyme: Pyruvate with NADH forms lactate with NAD+ through lactate dehydrogenase

A

Oxidoreductase

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24
Q

Classification of enzyme: Aspartate a-Ketogutarate to Oxaloacetate + Glutamate

A

Transferase

25
Q

Classification of enzyme: Acetylcholine with H2O to Acetate + Choline through Acetylcholinesterease

A

Hydrolase

26
Q

Classification of enzyme: cis-Aconitate to Isocitrate through Aconitase

A

Lyase

27
Q

Classification of enzyme: a-D-Glucose-6-phosphate to a-D-Fructose-6-phosphate through Phosphohexose isomerase

A

Isomerase

28
Q

Classification of enzyme: ATP + L-tyrosine + tRNA to L-tyrosyl-tRNA + AMP + PP through Tyrosine-tRNA synthetase

A

Ligase

29
Q

Enzyme activity is affected by (5)

A

Enzyme concentration
Substrate concentration
Temperature
pH
Presence of inhibitors

30
Q

Enzymes made of ribonucleic acid

A

Ribozymes

31
Q

Three types of inhibitors

A

Competitive
Non-competitive
Uncompetitive

32
Q

Type of inhibitor: when it enters the active site, the substrate cannot enter

A

Competitive

33
Q

Type of inhibitor: the inhibitor binds itself to a site other than the active site (allosterism), thereby changing the conformation of the active site

A

Noncompetitive

34
Q

Emphasize the shape of the active site (2)

A

Lock-and-key model and induced-fit model

35
Q

Just ____ amino acids participate in the active site in more than ____ of the enzymes studies to date

A

5, 65

36
Q

Amino acids that participate in active sites

A

His, Cys, Asp, Arg, Glu

37
Q

An enzyme-regulation process where the product of a series of enzyme-catalyzed reactions inhibits an earlier reaction in the sequence

A

Feedback control

38
Q

An inactive form of an enzyme that must have part of its polypeptide chain hydrolyzed and removed before it becomes active

A

Proenzyme (Zymogen)

39
Q

Example of proenzyme

A

Trypsin (digestive enzyme)

40
Q

Trypsin is sinthesized and stored as ____, which has no enzyme activity

A

Trypsinogen

41
Q

Trypsinogen only becomes active only after a six-amino fragment is hydrolyzed and removed from the ______

A

N-terminal end of its chain

42
Q

Removal of the fragment of trypsinogen changes ____ structure (2)

A

Primary and tertiary structure

43
Q

Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site

A

Allosterism

44
Q

Modulation: inhibition of an allosteric enzyme

A

Negative

45
Q

Modulation: stimulation of allosteric enzyme

A

Positive

46
Q

A substance that binds to an allosteric enzyme

A

Regulator

47
Q

The process of affecting enzyme activity by covalently modifying it

A

Protein modification

48
Q

Best known example of protein modification

A

Pyruvate kinase inactivated by phosphorylation to pyruvate kinase phosphate

49
Q

An enzyme that occurs in multiple forms; each catalyzes the same reaction

A

Isoenzyme

50
Q

Example of isoenzyme

A

Lactas dehydrogenase (LDH) catalyzes the oxidation of lactate to pyruvate

51
Q

Enzyme used for hepatitis

A

Alanine amino-transferase (ALT)

52
Q

Enzyme used for prostate cancer

A

Acid phosphatase

53
Q

Enzyme used for Liver or bone disease

A

Alkaline phosphatase (ALP)

54
Q

Enzyme used for pancreatic disease or mumps

A

Amylase

55
Q

Enzyme used for heart attack or hepatitis

A

Aspartate amino-transferase

56
Q

Enzyme used for heart attack (3)

A

Lactate dehydrogenase (LDH)
Creatine phosphokinase (CPK)
Phosphohexose isomerase (PHI)

57
Q

A molecule whose shape mimics the transition state of a substrate

A

Transition state analog

58
Q

Example of transition state analog

A

Proline racemase reaction (Pyrrole-2-carboxylate mimics the planar transition state)

59
Q

An antibody that has catalytic activity because it was created using a transition state analog as an immunogen

A

Abzyme

BioChem 1st Shifting (7 decks)

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