C13 Enzymes Flashcards

(70 cards)

0
Q

How are enzymes measured?

A

Activity

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1
Q

Enzymes

A

Special group of catalysts that are made up of proteins, speed up reaction

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2
Q

Catalyst

A

substances that lessen the amount of energy required for chemical reactions to occur

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3
Q

Enzyme (structure) Primary

A

amino acid sequence

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4
Q

Enzyme (Structure) Secondary

A

interaction between 2 locations on protein chain

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5
Q

Enzyme (structure) Tertiary

A

folding of chains (3D structure)

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6
Q

Enzyme (structure) Quadernary

A

2 or more separate polypeptide chains

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7
Q

Active site

A

physical location on the enzyme molecule which interacts w/ substrate molecule

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8
Q

Allosteric site

A

non active site, but which may interact w/ other substances to change overall enzyme 3D shape

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9
Q

Isoenzyme

A

structurally diff enzymes (proteins) but which catalyze the same chemical reactions

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10
Q

Cofactor

A

a non protein substance required for normal enzyme activity, maintain enzyme 3D structure, critical for enzyme function

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11
Q

2 types of cofactors?

A

activators (inorganic) & coenzyme (organic)

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12
Q

Holoenzyme

A

Enzyme+coenzyme (prosthetic group)=active enzyme

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13
Q

Proenzyme

A

enzyme-coenzyme=active enzyme

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14
Q

The amount of energy required to stimulate molecules to break their chemical bonds and form new bonds is the ___.

A

activation energy

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15
Q

absolute type enzymes

A

catalyzes only 1 specific substrate

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16
Q

Group type enzymes

A

catalyzes reactions of a particular chemical group

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17
Q

Bond type enzyme

A

catalyzes reactions of particular chemical bonds

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18
Q

Steroisomerism

A

catalyzes reactions of steroisomers

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19
Q

What does the substrate do?

A

saturates enzymes (all enzymes react with excess substrate)

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20
Q

Enzyme activity

A

the rate at which an enzyme catalyzes a chemical reaction

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21
Q

Why is activity measured under Zero Order conditions?

A

because this is where the reaction rate is dependent on the work (activity) of the enzyme

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22
Q

Competitive inhibitors

A

substances that bind at the enzyme’s site, competes with substrate for the active site, addition of additional substrate increases the reaction rate

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23
Q

Non-competitive inhibitors

A

substances that bind at an enzyme’s non-active site, enzyme 3d shape is altered, decreasing enzyme activity, may bind substrate but additional substrate has no effect

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24
uncompetitive inhibitor
substances that bind with enzyme-substrate complex
25
How can enzyme activity be measured?
increase of product, decrease of substrate, decrease of co-enzymes, and increase of altered co-enzyme
26
Fixed-Time Assay
substrate concentration is measured at set time intervals to determine enzyme activity
27
What is a slight delay from the beginning of the reaction to max velocity?
lag phase
28
substrate depletion
extreme elevations in enzyme activity may deplete the substrate between measured intervals, causes falsely decreased activity results
30
Multipoint Continuous Monitoring (Kinetic Assay)
continuous measurements of substrate-product concentration are recorded by the spectrophotometer of an automated analyzer
31
What is the common unit of enzyme activity?
International Unit (IU)
32
1 IU
that amount of enzyme that will convert 1 micro-mole of substrate to product per minute under defined conditions
33
NADH
Common co-enzyme, absorbs light at 340 NM
34
Why are enzymes used as reagents?
to measure other non-enzymes
35
High concentrations of CPK are found in?
muscle, cardiac & brain tissues
36
Increased CPK is associated with?
damage to the muscle, cardiac, and brain tissues
37
Increased CPK is useful to diagnose?
AMIs and skeletal muscle disease (muscular dystrophy)
38
How many isoenzymes does CPK have?
3
39
CK-BB
Brain
40
CK-MB
Cardiac
41
CK-MM
Skeletal muscle
42
Because of CK-MBs association with cardiac tissue, increased CPK-MB (>_6% Total CPK activity) is a strong indication of?
AMI
43
Lactate dehydrogenase is found in what tissues?
skeletal muscle, cardiac muscle, renal tissue, and RBCs
44
Plasma LDH is elevated in what conditions?
Liver disease, cancers, AMI, hemolytic diseases
45
How many isoenzymes does LDH have?
5
46
LD-1
(HHHH) Cardiac, RBCs
47
LD-2
(HHHM)
48
LD-3
(HHMM) lung, spleen, pancreas
49
LD-4
(HMMM) hepatic, skeletal
50
LD-5
(MMMM)
51
Aspartate aminotransferase high concentrations are found in?
skeletal muscle, cardiac muscle, liver tissue, and lung tissue
52
Alanine aminotransferase has the highest activity in the?
liver
53
alkaline phosphate does what?
removes phosphates from organic compounds
54
alkaline phosphate has higher concentrations in?
bone and liver
55
what group of people have higher ranges of alkaline phosphate?
children, because they are still growing
56
Amylase catalyzes breakdown of?
starch and glycogen to glucose
57
High concentrations of amylase are found in?
pancreas and saliva
58
amylase is filtered into the?
urine
59
increased plasma or urine amylase is very sugguestive of?
pancreatitis or pacreatic malignancy
60
Gamma glutamyltransferase has high concentrations in the?
liver
61
increased plasma GGT is associated with?
hepatobiliary disease & alcoholic cirrhosis
62
Lipase hydrolyzes (break down)?
fat
63
high concentrations of lipase are found in?
pancreas
64
pseudocholinesterase is considered a screening test for exposure to?
organophosphate exposure (pesticides)
65
3 step in diagnosing AMI?
1-symptoms, physical exam, patient history 2-EKG 3-lab tests
66
Myoglobin is a soluble?
heme protein
67
two forms of Troponin?
Troponin I and Troponin T
68
Cardiac enzymes, "CAL 911"
CPK, AST, LDH
69
What is the "triage" used for?
common commercial test package that quantitates the 3 most significant lab markers for AMI: CK-MB, Troponin I, and Myoglobin
70
How are enyzmes measured?
At Zero Order