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Midterm Exam > PBIO Enzymes > Flashcards

PBIO Enzymes Flashcards

1
Q

Greek word of enzyme

A

En (in) Zyme yeast

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2
Q

Are catalysts and are not consumed in the reactions

A

Enzymes

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3
Q

Are proteins that act as a catalyst for biochemical reactions

A

Enzymes

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4
Q

The human body has (# of enzymes)

A

1000s

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5
Q

Are the most effective catalysts known

A

Enzymes

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6
Q

Most enzymes are

A

Globular proteins

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7
Q

Undergo all the reactions of proteins including denaturation

A

Enzymes

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8
Q

Enzyme activity is dramatically affected by

A

Alterations in pH
Temperature
Other protein denaturants

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9
Q

Two types of enzymes

A

Simple and conjugated

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10
Q

Composed of only proteins

A

Simple enzyme

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11
Q

Has a nonprotein part in addition to a proteinn part

A

Conjugated enzyme

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12
Q

Protein part of a conjugated enzyme

A

Apoenzyme

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13
Q

Nonprotein part of a conjugated enzyme

A

Cofactor

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14
Q

Biochemically active conjugated enzyme

A

Holoenzyme

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15
Q

Components of holoenzyme

A

Apoenzyme+cofactor

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16
Q

Are important for chemically reactive enzymes
And are small organic molecules or inorganic ions

A

Cofactors

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17
Q

Organic molecule cofactors are also called

A

Co-enzymes or co-substrates

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18
Q

Co-enzymes/co-substrates are derived

A

Dietary vitamins

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19
Q

Typical metal ion cofactors

A

Zn2+,Mg2+,Mn2-and Fe2-

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20
Q

Inorganic ion cofactors derived from dietary minerals

A

Cofactors

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21
Q

Is the reactant in an enzyme catalyzed reaction

A

Substrate

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22
Q

The substrate is the substance upon which the

A

Enzyme acts.

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23
Q

Six major classes of enzymes

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerase
Ligases

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24
Q

Oxidation reductions

A

Oxidoreductases

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25
Q

Functional group of transfer reactions

A

Transferases

26
Q

Hydrolysis reactions

A

Hydrolases

27
Q

Reactions involving addition or removal of groups form double bonds

A

Lyases

28
Q

Isomerisation reactions

A

Isomerase

29
Q

Reactions involving bond formation couples with atp hydrolysis

A

Ligases

30
Q

An oxidoreductase enzyme

A

Catalyzes an oxidation-reduction reaction

31
Q

An oxidoreductase requires a coenzyme that is either

A

Oxidized or reduced

32
Q

It is an enzyme that catalyzes the transfer of a functional group from one molecule to another

A

Transferase

33
Q

Catalyze transfer of an amino group to a substrate

A

Transaminases

34
Q

Catalyze transfer of a phosphate group from adenosine triphosphate ATP to a substrate

A

Kinases

35
Q

Is an enzyme that catalyzes a hydrolysis reaction

A

Hydrolase

36
Q

Hydrolase- the reaction involves

A

Addition of a water to molecule to a bond to cause bond breakage

37
Q

Are central to the process of digestion

A

Hydrolysis reactions/hydrolase

38
Q

Effect the breaking of peptide linkages in proteins

A

Proteases

39
Q

Effect the breaking of ester linkages in triacylglycerols

A

Lipases

40
Q

An enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

A

Lyase EC4

41
Q

Effects the removal of the components of water from a double bond

A

Dehydratase

42
Q

Effects the addition of the components of water to a double bonds

A

Hydratase

43
Q

An enzyme that catalyzes the isomerization (rearrangement of atoms) reactions

A

Isomerase

44
Q

An enzyme that catalyzes the formation of a bond between 2 molecules involving ATP hydrolysis

A

Ligase

45
Q

Relatively small part of an enzyme structure that is actually involved in catalysis

A

Active site

46
Q

Place where substrate binds to enzyme
Formed due to folding and bending of the protein
Usually a crevice like location in the enzyme
Some enzymes have more than one active site

A

Enzyme active site

47
Q

Intermediate reaction species formed when substrate binds with the active site.
Needed fo the activity of enzyme
Orientation and proximity is favorable and reaction is fast,

A

Enzyme substrate complex

48
Q

Two models for substrate binding to enzyme

A

Lock and key model
Induced fit model

49
Q

Enzyme has a pre determined shape for active site
Only substrate of a specific shape can bind with active site.

A

Lock and key model

50
Q

Substrate contact with enzyme will change the shape of the active site
Allows small changes in space to accomodate substrate (e.g. how a hand fits into a glove)

A

Induced fit model

51
Q

Forces that determine substrate binding

A

H-bonding
Hydrophobic interactions
Electrostatic interactions

52
Q

An enzyme will catalyze a particular reaction for only one substrate
Most restrictive of all specifities not common

A

Absolute specifity

53
Q

Example of absolute specifity

A

Urease

54
Q

An enzyme can distinguish between stereoisomers .
Chirality is inherent in an active site (amino acids are chiral compounds)

A

Stereochemical specifity

55
Q

Catalyzes reactions of L-amino acids but not of D-amino acids

A

L-amino acid oxidase

56
Q

Involves structurally similar compounds that have the same functional groups

A

Group specificity

57
Q

Cleaves amino acids one at a time frome the carboxyl end of the peptide chain

A

Carboxypeptidase

58
Q

Involves a particular type of bond irrespective of the structural features in the vicinity of the bond

A

Linkage specificity

59
Q

Cosidered most general of enzyme specifities

A

Linkage specificity

60
Q

Hydrolyze phosphate ester bonds in all types of phosphate esters

A

Phosphatases

Midterm Exam (4 decks)

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