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
Functional group of transfer reactions
Transferases
26
Hydrolysis reactions
Hydrolases
27
Reactions involving addition or removal of groups form double bonds
Lyases
28
Isomerisation reactions
Isomerase
29
Reactions involving bond formation couples with atp hydrolysis
Ligases
30
An oxidoreductase enzyme
Catalyzes an oxidation-reduction reaction
31
An oxidoreductase requires a coenzyme that is either
Oxidized or reduced
32
It is an enzyme that catalyzes the transfer of a functional group from one molecule to another
Transferase
33
Catalyze transfer of an amino group to a substrate
Transaminases
34
Catalyze transfer of a phosphate group from adenosine triphosphate ATP to a substrate
Kinases
35
Is an enzyme that catalyzes a hydrolysis reaction
Hydrolase
36
Hydrolase- the reaction involves
Addition of a water to molecule to a bond to cause bond breakage
37
Are central to the process of digestion
Hydrolysis reactions/hydrolase
38
Effect the breaking of peptide linkages in proteins
Proteases
39
Effect the breaking of ester linkages in triacylglycerols
Lipases
40
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
Lyase EC4
41
Effects the removal of the components of water from a double bond
Dehydratase
42
Effects the addition of the components of water to a double bonds
Hydratase
43
An enzyme that catalyzes the isomerization (rearrangement of atoms) reactions
Isomerase
44
An enzyme that catalyzes the formation of a bond between 2 molecules involving ATP hydrolysis
Ligase
45
Relatively small part of an enzyme structure that is actually involved in catalysis
Active site
46
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
Enzyme active site
47
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,
Enzyme substrate complex
48
Two models for substrate binding to enzyme
Lock and key model Induced fit model
49
Enzyme has a pre determined shape for active site Only substrate of a specific shape can bind with active site.
Lock and key model
50
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)
Induced fit model
51
Forces that determine substrate binding
H-bonding Hydrophobic interactions Electrostatic interactions
52
An enzyme will catalyze a particular reaction for only one substrate Most restrictive of all specifities not common
Absolute specifity
53
Example of absolute specifity
Urease
54
An enzyme can distinguish between stereoisomers . Chirality is inherent in an active site (amino acids are chiral compounds)
Stereochemical specifity
55
Catalyzes reactions of L-amino acids but not of D-amino acids
L-amino acid oxidase
56
Involves structurally similar compounds that have the same functional groups
Group specificity
57
Cleaves amino acids one at a time frome the carboxyl end of the peptide chain
Carboxypeptidase
58
Involves a particular type of bond irrespective of the structural features in the vicinity of the bond
Linkage specificity
59
Cosidered most general of enzyme specifities
Linkage specificity
60
Hydrolyze phosphate ester bonds in all types of phosphate esters
Phosphatases