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cc lec 2 > P1: Introduction to Enzymatics > Flashcards

P1: Introduction to Enzymatics Flashcards

1
Q

Study of enzymes: activity of enzymes, chemical
reaction they create, clinical uses

A

Enzymology

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2
Q

○ present inside tissues and cells
○ Not common in the circulation

A

Biological catalyst

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3
Q

○ Without enzymes, higher level of energy and
more time is needed for the reaction to
occur

A

Hasten Chemical reactions

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4
Q

○ Enzyme will leave the reaction intact

A

Are not consumed during reactions

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5
Q

● Do not undergo a chemical change after the
reactions

A

Enzymes

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6
Q

_____________ is not diagnostic to a certain disease, but it is useful in specifying which organ is
affected

A

Enzyme testing

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7
Q

recognizes and catalyzes a single
substrate

A

Absolute

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8
Q

Give me the three enzyme specificity

A
  1. Absolute
  2. Group
  3. Linkage
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9
Q

Recognizes and catalyzes a group of substrates that have specific functional
groups

A

Group

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10
Q

Recognizes and catalyzes a group of substrates that have a particular type of
bond

A

Linkage

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11
Q

NOMENCLATURE OF ENZYMES

A
  1. Substrate + ase
  2. Reaction it catalyzes
  3. Enzyme commission Nomenclature
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12
Q

● The names of some enzymes do not end in -ase

A

pepsin and trypsin

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13
Q

active form of pepsinogen

A

pepsin

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14
Q

active form of trypsinogen

A

trypsinogen

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15
Q

OTHLIL CLASSIFICATION OF ENZYMES

A

OTHLIL
1. oxidoreductases
2. transferases
3. hydrolases
4. lyases
5. isomerases
6. ligases

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16
Q

___________________- removal of H ion / electrons

A

Oxidation

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17
Q

_____________________ - acceptance of H ion / electrons

A

Reduction

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18
Q

Transfer of functional groups other than hydrogen
from one substrate to another

A

Transferases

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19
Q

● Hydrolysis of various bonds

A

hydrolases

20
Q

Addition of water to a bond resulting in bond
breakage

A

hydrolases

21
Q

Catalyze the removal of groups from substrates
without hydrolysis or oxidation

A

lyases

22
Q

the product contains double bonds or a ring

A

lyases

23
Q

No water involved; structure is broken down
by enzyme alone

A

lyases

24
Q

○ Complex substrate structure is broken down
into simpler form

A

lyases

25
Q

Rearrange the functional groups within a molecule
and catalyze the conversion of one isomer into
another

A

isomerases

26
Q

Catalyze the joining of two large molecules by
forming a new chemical bond

A

ligases

27
Q

Site where enzyme binds to the substrate

A

active site

28
Q

● Has the same shape as substrate

A

active site

29
Q

● Two types of theory : __________ and ___________

A

lock and key, induced fit

30
Q

● Binding site on enzyme where activators and
inhibitors bind

A

allosteric site

31
Q

Changes the structure of the active site to prevent
substrate binding

A

Inhibitor

32
Q

Changes the shape of the active site to the
appearance of the substrate to promote binding

A

activator

33
Q

Acted upon by the enzyme
● Specific

A

substrate

34
Q

● Different form but with the same action

A

isoenzyme

35
Q

● Non-protein molecule

A

cofactor

36
Q

● Facilitate enzymatic reactions

A

cofactor

37
Q

● Not all reactions require cofactors

A

cofactor

38
Q

Without cofactors: _______________
With cofactors: ______________

A

inactive apoenzyme
active holoenzyme

39
Q

tightly bound
Metal ions (activators) or organic molecules
● Change the configuration of the enzyme/link
substrate to enzyme/coenzyme

A

Prosthetic groups

40
Q

● loosely bound
● Organic molecules
● “second substrate” for enzyme reactions

A

Coenzymes

41
Q

Polypeptide portion
Inactive enzyme

A

apoenzyme

42
Q

Enzyme that requires but does not have
cofactor yet; without cofactor, substrate
cannot bind to enzyme

A

apoenzymes

43
Q

● Also known as zymogen

A

proenzyme

44
Q

● Enzyme precursor; inactive

A

proenzyme

45
Q

● Converted by proteolysis

A

proenzyme

46
Q
A

cc lec 2 (15 decks)

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