PRELIM LESSON#1: 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

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
1st digit =_______ ○ Based on the OTHLIL classification ● 2nd digit = _______ ● 3rd and 4th =_________
class subclass serial number
26
The names of some enzymes do not end in -ase ex. _______, _________
pepsin, trypsin
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__________ - active form of pepsinogen
Pepsin
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_____________- active form of trypsinogen
Trypsin
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2) Reaction it catalyzes (5 examples)
ORHDD Oxidation reduction hydrolysis dehydrogenase decarboxylase
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1) Substrate + -ase (5 examples)
Lipids Esterase Protein Amylose Lactose
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OTHLIL CLASSIFICATION OF ENZYMES
OTHLIL ● Oxidoreductases ● Transferases ● Hydrolases ● Lyases ● Isomerases ● Ligases
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removal of H ion / electrons
Oxidation
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acceptance of H ion / electrons
Reduction
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Ex. E.C. 1.1.1.27: L-lactate NAD+ Oxidoreductase ○ Lactate dehydrogenase
OXIDOREDUCTASES
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Transfer of functional groups other than hydrogen from one substrate to another
2) TRANSFERASES
36
Ex. E.C. 2.6.1.1 : L-Aspartate: 2-Oxaloglutarate Aminotransferase ○ Aspartate Aminotransferase
TRANSFERASES
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Hydrolysis of various bonds
HYDROLASES
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○ Addition of water to a bond resulting in bond breakage
3) HYDROLASES
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Ex. E.C. 3.1.1.3 : triacylglycerol lipase
3) HYDROLASES
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Catalyze the removal of groups from substrates without hydrolysis or oxidation
4) LYASES
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the product contains double bonds or a ring
4) LYASES
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Rearrange the functional groups within a molecule and catalyze the conversion of one isomer into another Ex. Phosphoglycerate mutase
ISOMERASES
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Catalyze the joining of two large molecules by forming a new chemical bond Ex. DNA ligase
6) LIGASES
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● Site where enzyme binds to the substrate
ACTIVE SITE
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● Has the same shape as substrate ● Two types: lock and key, induced fit
ACTIVE SITE
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Binding site on enzyme where activators and inhibitors bind
ALLOSTERIC SITE
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Changes the structure of the active site to prevent substrate binding
Inhibitor
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Changes the shape of the active site to the appearance of the substrate to promote binding
Activator
49
● Acted upon by the enzyme ● Specific
SUBSTRATE
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Different form but with the same action
ISOENZYME
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● Non-protein molecule ● Facilitate enzymatic reactions ● Not all reactions require cofactors
COFACTOR
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Some enzymes require cofactors ● Without cofactors: ____________ ● With cofactors: _____________
Some enzymes require cofactors ● Without cofactors: inactive apoenzyme ● With cofactors: active holoenzyme
53
● tightly bound ● Metal ions (activators) or organic molecules ● Change the configuration of the enzyme/link substrate to enzyme/coenzyme
PROSTHETIC GROUPS
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● loosely bound ● Organic molecules ● "second substrate" for enzyme reactions
COENZYMES
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what are the two TYPES OF COFACTORS
PROSTHETIC GROUPS and COENZYMES
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● Polypeptide portion ● Inactive enzyme
APOENZYME
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Apoenzyme + Coenzyme
HOLOENZYME
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● Also known as zymogen ● Enzyme precursor; inactive ● No active site ● Converted by proteolysis Ex: Trypsinogen to Trypsin ________________________
PROENZYME Chymotrypsinogen to Chymotrypsin
59