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CLINICAL CHEMISTRY LEC 2 (PRELIM - FINALS) > PRELIM LESSON#1: INTRODUCTION TO ENZYMATICS > Flashcards

PRELIM LESSON#1: INTRODUCTION TO ENZYMATICS Flashcards

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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

ENZYMES

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3
Q

_________ act as Biological catalysts

A

ENZYMES

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4
Q

Hasten chemical reactions

A

ENZYMES

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5
Q

___________are not consumed during 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

Enzyme + Substrate = __________

A

Product

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8
Q

_____________are categorized according to what they catalyze

A

Enzymes

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9
Q

recognizes and catalyzes a single substrate

A

ABSOLUTE

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10
Q

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

A

GROUP

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11
Q

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

A

LINKAGE

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12
Q

Enzyme specificity has three groups

A

Absolute
Group
Linkage

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13
Q

3 NOMENCLATURE OF ENZYMES

A

SRE
1) Substrate + -ase
2) Reaction it catalyzes
3) Enzyme Commission Nomenclature (E.C.)

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14
Q

Lipid = __________

A

lipase

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15
Q

Ester = __________

A

esterase

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16
Q

Protein = ________

A

protease

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17
Q

Amylose = ___________

A

amylase

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18
Q

Lactose = ___________

A

lactase

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19
Q

Oxidation = __________

A

oxidase

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20
Q

Reduction = ___________

A

reductase

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21
Q

Hydrolysis = ___________

A

hydrolase

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22
Q

_________ = remove hydrogen atoms

A

Dehydrogenase

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23
Q

_________ = remove carboxyl groups

A

Decarboxylase

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24
Q

ex. E.C. 1.1.1.21

A

3) Enzyme Commission Nomenclature (E.C.)

25
Q

1st digit =_______
○ Based on the OTHLIL classification
● 2nd digit = _______
● 3rd and 4th =_________

A

class
subclass
serial number

26
Q

The names of some enzymes do not end in -ase

ex. _______, _________

A

pepsin, trypsin

27
Q

__________ - active form of pepsinogen

A

Pepsin

28
Q

_____________- active form of trypsinogen

A

Trypsin

29
Q

2) Reaction it catalyzes

(5 examples)

A

ORHDD

Oxidation
reduction
hydrolysis
dehydrogenase
decarboxylase

30
Q

1) Substrate + -ase

(5 examples)

A

Lipids
Esterase
Protein
Amylose
Lactose

31
Q

OTHLIL CLASSIFICATION OF ENZYMES

A

OTHLIL
● Oxidoreductases
● Transferases
● Hydrolases
● Lyases
● Isomerases
● Ligases

32
Q

removal of H ion / electrons

A

Oxidation

33
Q

acceptance of H ion / electrons

A

Reduction

34
Q

Ex. E.C. 1.1.1.27: L-lactate NAD+ Oxidoreductase
○ Lactate dehydrogenase

A

OXIDOREDUCTASES

35
Q

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

A

2) TRANSFERASES

36
Q

Ex. E.C. 2.6.1.1 : L-Aspartate: 2-Oxaloglutarate
Aminotransferase
○ Aspartate Aminotransferase

A

TRANSFERASES

37
Q

Hydrolysis of various bonds

A

HYDROLASES

38
Q

○ Addition of water to a bond resulting in bond breakage

A

3) HYDROLASES

39
Q

Ex. E.C. 3.1.1.3 : triacylglycerol lipase

A

3) HYDROLASES

40
Q

Catalyze the removal of groups from substrates without hydrolysis or oxidation

A

4) LYASES

41
Q

the product contains double bonds or a ring

A

4) LYASES

42
Q

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

Ex. Phosphoglycerate mutase

A

ISOMERASES

43
Q

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

Ex. DNA ligase

A

6) LIGASES

44
Q

● Site where enzyme binds to the substrate

A

ACTIVE SITE

45
Q

● Has the same shape as substrate
● Two types: lock and key, induced fit

A

ACTIVE SITE

46
Q

Binding site on enzyme where activators and inhibitors bind

A

ALLOSTERIC SITE

47
Q

Changes the structure of the active site to prevent substrate binding

A

Inhibitor

48
Q

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

A

Activator

49
Q

● Acted upon by the enzyme
● Specific

A

SUBSTRATE

50
Q

Different form but with the same action

A

ISOENZYME

51
Q

● Non-protein molecule
● Facilitate enzymatic reactions
● Not all reactions require cofactors

A

COFACTOR

52
Q

Some enzymes require cofactors
● Without cofactors: ____________
● With cofactors: _____________

A

Some enzymes require cofactors
● Without cofactors: inactive apoenzyme
● With cofactors: active holoenzyme

53
Q

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

A

PROSTHETIC GROUPS

54
Q

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

A

COENZYMES

55
Q

what are the two TYPES OF COFACTORS

A

PROSTHETIC GROUPS and COENZYMES

56
Q

● Polypeptide portion
● Inactive enzyme

A

APOENZYME

57
Q

Apoenzyme + Coenzyme

A

HOLOENZYME

58
Q

● Also known as zymogen
● Enzyme precursor; inactive
● No active site
● Converted by proteolysis

Ex: Trypsinogen to Trypsin
________________________

A

PROENZYME

Chymotrypsinogen to Chymotrypsin

59
Q
A

CLINICAL CHEMISTRY LEC 2 (PRELIM - FINALS) (2 decks)

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