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Clinical Chemistry Review > Enzymes > Flashcards

Enzymes Flashcards

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1
Q

Serum ; Reagent

A

Enzyme concentration ; Substrate concentration

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2
Q

↑ Enzyme concentration =

Enzyme > substrate, substrate =

A

↑ reaction rate

↑ reaction rate

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3
Q

When substrate concentration reaches a maximal value, higher concentration of substrate no longer results in increased rate of reaction

A

Saturation kinetics

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4
Q

Nonprotein entities

A

Cofactors

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5
Q

Organic compound (Ex. NADP)

A

Coenzymes

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6
Q

↑Coenzyme =

A

↑ Velocity

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7
Q

Inorganic ions

A

Activators

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8
Q

Alters spatial configuration of the enzyme for proper substrate binding

A

Activators

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9
Q

Ex. Ca2+ (#1 activator), Zn2+ (LDH), Cl- (AMS), Mg2+ (CK, ALP)

A

Activators

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10
Q

Inorganic ion attached to a molecule

A

Metalloenzymes

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11
Q

Ex. Catalase, cytochrome oxidase

A

Metalloenzymes

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12
Q

Interferes with the enzymatic reactions

A

Inhibitors

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13
Q

Binds to the active site of an enzyme

A

Competitive inhibitor

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14
Q

Reversible (Substrate > Inhibitor)

A

Competitive inhibitor

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15
Q

Binds to the allosteric site (cofactor site)

A

Noncompetitive inhibitor

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16
Q

Irreversible

A

Noncompetitive inhibitor

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17
Q

Binds to the enzyme-substrate complex

A

Uncompetitive inhibitor

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18
Q

↑ Substrate =

A

↑ ES = ↑ Inhibition

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19
Q

Same catalytic reactions but slightly different molecular structures ; Fractionation

A

Isoenzymes

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20
Q

Ex. NADP

A

Coenzymes

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21
Q

= optimum temperature for enzyme activity

A

37’C

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22
Q

↑ Temperature =

A

↑ Reaction rate (↑ movement of molecules)

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23
Q

Denaturation of enzymes

A

40-50’C

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24
Q

Inactivation of enzymes

A

60-65’C

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25
Q

For every 10OC increase in temperature, there will be a two-fold increase in enzyme activity

A

Temperature coefficient (Q10)

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26
Q

Most physiologic reactions occur in the pH range of

A

7-8

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27
Q

Storage
Enzymes: = for longer period of time
Substrate and Coenzymes:
LDH (LD4 & 5):

A

-20’C

2-8’C

Room temperature

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28
Q

Mostly increases enzyme concentration

A

Hemolysis

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29
Q

Decreases enzyme concentration

A

Lactescence or milky specimen

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30
Q

Enzyme nomenclature
1st digit:
2nd and 3rd digits:
4th digit(s):

A

classification

subclass

serial number

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31
Q

Enzyme classification

A

“OTHLIL”
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

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32
Q

Redox reaction

A

Oxidoreductases

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33
Q

Dehydrogenases

A

-Cytochrome oxidase
-LDH
-MDH
-Isocitrate dehydrogenase
-G-6-PD

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34
Q

Transfer of a chemical group other than hydrogen from 1 substrate to another

A

Transferases

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35
Q

Kinases, Transaminases, Aminotransferases:

A

-CK
-GGT
-AST
-ALT
-OCT

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36
Q

Hydrolysis/splitting by addition of water

A

Hydrolases

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37
Q

Esterases

A

-ACP
-ALP
-CHS
-LPS

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38
Q

Peptidases

A

-Trypsin
-Pepsin
-LAP

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39
Q

Glycosidases

A

-AMS
-Galactosidases

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40
Q

Removal of groups w/o hydrolysis (product contains double bonds)

A

Lyases

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41
Q

Decarboxylases

A

-Glutamate decarboxylase
-Pyruvate decarboxylase
-Tryptophan decarboxylase

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42
Q

Intramolecular arrangements

A

Isomerases

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43
Q

Glucose phosphate isomerase

A

Isomerases

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44
Q

Ribose phosphate isomerase

A

Isomerases

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45
Q

Joining of 2 substrate molecules

A

Ligases

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46
Q

Synthases

A

Ligases

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47
Q

Water-free cavity

A

Active site

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48
Q

Where the substrate interacts

A

Active site

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49
Q

Cavity other than the active site

A

Allosteric site

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50
Q

May bind regulatory molecules

A

Allosteric site

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51
Q

Coenzyme that is bound tightly to the enzyme

A

Prosthetic group

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52
Q

Apoenzyme + Prosthetic group

A

Holoenzyme

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53
Q

Inactive form of enzyme

A

Zymogen/proenzyme

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54
Q

Shape of the key (substrate) must fit into the lock (enzyme)

A

Emil Fisher’s/Lock and Key theory

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55
Q

Based on the substrate binding to the active site of the enzyme

A

Kochland’s/Induced fit theory

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56
Q

Acceptable theory

A

Kochland’s/Induced fit theory

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57
Q

Enzymes catalyze reactions by lowering the activation energy level that the substrate must reach for the reaction to occur

A

Enzyme kinetics

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58
Q

Enzyme combines w/ only 1 substrate and catalyzes only 1 reaction

A

Absolute specificity

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59
Q

Enzymes combine w/ all the substrates in a chemical group

A

Group specificity

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60
Q

Enzymes reacting w/ specific chemical bonds

A

Bond specificity

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61
Q

Reaction rate depends only on enzyme concentration Independent on substrate concentration

A

Zero-order reaction

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62
Q

Reaction rate is directly proportional to substrate concentration

A

First-order reaction

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63
Q

Independent on enzyme concentration

A

First-order reaction

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64
Q

Measurement of enzyme activity

A

Change in substrate concentration
Change in product concentration
Change in coenzyme concentration

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65
Q

1 micromole of substrate/minute

A

International Unit

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66
Q

Unit 1 mole of substrate/second

A

Katal

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67
Q

Absorbance is made at 10-second intervals for 100 seconds

A

Nonkinetic assay

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68
Q

pH = 10.5 ; 405nm

A

Alkaline Phosphatase

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69
Q

Electrophoresis: (+) Liver  Bone (Regan)  Placenta  Intestine (-)

A

Alkaline Phosphatase

70
Q

Heat fractionation: (Δ Stable) Regan  Placenta  Intestine  Liver  Bone (Δ Labile)

A

Alkaline Phosphatase

71
Q

Inhibits Regan, placental and intestinal ALP

A

Phenylalanine

72
Q

Inhibits Nagao ALP

A

L-leucine

73
Q

Inhibits liver and bone ALP

A

Levamisole

74
Q

Inhibits bone ALP Methods (ALP)

A

3M urea

75
Q

= Increased ALP

A

Low temperature

76
Q

Methods (ALP)

A
  1. Bowers and McComb (PNPP) – IFCC recommended
  2. Bessy, Lowry and Brock (PNPP)
  3. Bodansky, Shinowara, Jones, Reinhart = BGP (beta glycerophosphate)
  4. King and Armstrong = PP (phenylphosphate)
  5. Klein, Babson & Read = Buffered PPP (phenolphthalein phosphate)
  6. Huggins and Talalay = PPDP (phenolphthalein diphosphate)
  7. Moss = ANP (alpha naphthol phosphate)
77
Q

– IFCC recommended

A
  1. Bowers and McComb
78
Q

(PNPP)

A
  1. Bowers and McComb
  2. Bessy, Lowry and Brock
  3. Shinowara
79
Q

= BGP (beta glycerophosphate)

A
  1. Bodansky, Shinowara, Jones, Reinhart
80
Q

= PP (phenylphosphate)

A
  1. King and Armstrong
  2. Gutman and Gutman
81
Q

= Buffered PPP (phenolphthalein phosphate)

A
  1. Klein, Babson & Read
82
Q

= PPDP (phenolphthalein diphosphate)

A
  1. Huggins and Talalay
83
Q

= ANP (alpha naphthol phosphate)

A
  1. Moss
84
Q

Sprue, Hyperparathyroidism, Rickets (children) and osteomalacia (adults)

A

Increased ALP

85
Q

pH = 5.5 ; 405nm

A

Acid Phosphatase

86
Q

Sources: Prostate (major), RBC, platelets, bone

A

Acid Phosphatase

87
Q

pH 7.5 ; 340nm

A

Aspartate Aminotransferase (AST/SGOT)

88
Q

Sources: Cardiac tissue > Liver > Skeletal muscle > Kidney, pancreas, RBCs

A

Aspartate Aminotransferase (AST/SGOT)

89
Q

pH 7.5 ; 340nm

A

Alanine Aminotransferase (ALT/SGPT)

90
Q

Major Source: Liver

A

Alanine Aminotransferase (ALT/SGPT)

91
Q

Inhibited by L-tartrate ions

A

Prostatic ACP

92
Q

Inhibited by cupric and formaldehyde ions

A

RBC ACP

93
Q

Room temperature (1-2 hrs) =

A

decreased ACP

94
Q

= specific substrate, substrate of choice (endpoint)

A

Thymolphthalein monophosphate

95
Q

= preferred for continuous monitoring methods

A

Alpha-naphthyl phosphate

96
Q

Methods (ACP)

A
  1. Gutman and Gutman = PP
  2. Shinowara = PNPP
97
Q

= ANP (continuous monitoring)

A
  1. Babsonm Read and Phillips
98
Q

= Thymolphthalein monophosphate (endpoint)

A
  1. Roy and Hillman
99
Q

Methods (AST and ALT)

A
  1. Karmen method = Kinetic
  2. Reitman and Frankel = Endpoint
100
Q

Reitman and Frankel
-Color developer:
-Color intensifier:

A

DNPH

0.4N NaOH

101
Q

Increased Transaminases DeRitis ratio (ALT:AST) >1.0 =

A

Acute hepatitis (Highest)

102
Q

Increased Transaminases ↑ 20x =

A

viral or toxic hepatitis

103
Q

Increased Transaminases Moderate elevation =

A

chronic hepatitis, hepatic cancer, IM

104
Q

Increased Transaminases Slight elevation =

A

Hepatic cirrhosis, alcoholic hepatitis, obstructive jaundice

105
Q

Smallest enzyme (appears in urine)

A

Amylase

106
Q

Earliest pancreatic marker

A

Amylase

107
Q

: most predominant pancreatic AMS isoenzyme in AP

A

P3

108
Q

Amylase Isoenzymes:

A

S-type (ptyalin): anodal
P-type (amylopsin): cathodal

109
Q

Samples w/ high activity of AMS should be diluted w/ [?] to prev. inactivation

A

NaCl

110
Q

= inhibited by wheat germ lectin

A

Salivary AMS

111
Q

AMS Substrate:

A

Starch

112
Q

Reducing sugars produced

A

Saccharogenic

113
Q

Classic reference method (SU)

A

Saccharogenic

114
Q

Degradation of starch

A

Amyloclastic

115
Q

Increase in color intensity

A

Chromogenic

116
Q

Continuous-monitoring technique

A

Coupled-enzyme

117
Q

Late marker (AP)

A

Lipase

118
Q

Most specific pancreatic marker

A

Lipase

119
Q

LPS Substrate:

A

Olive oil/Triolein

120
Q

Methods (LPS)

A
  1. Cherry Crandal (Reference method)
  2. Tietz and Fiereck
  3. Peroxidase coupling (most commonly used method)
121
Q

LPS
(Reference method)
(most commonly used method)

A
  1. Cherry Crandal
  2. Peroxidase coupling
122
Q

Lacks specificity

A

Lactate dehydrogenase

123
Q

RBC: 150x than in serum

A

Lactate dehydrogenase

124
Q

Lactate dehydrogenase Sources:

A

LD1 (α-HBD) and LD2 = Heart, RBC, Kidneys
LD3 = pancreas, lungs, spleen
LD4 an LD5 = liver and muscle
LD6 = alcohol dehydrogenase

125
Q

= Heart, RBC, Kidneys

A

LD1 (α-HBD) and LD2

126
Q

= pancreas, lungs, spleen

A

LD3

127
Q

= liver and muscle

A

LD4 an LD5

128
Q

= alcohol dehydrogenase

A

LD6

129
Q

Methods (LDH)

A
  1. Wacker method (forward/direct)
  2. Wrobleuski LaDue (reverse/indirect)
  3. Wrobleuski Cabaud
  4. Berger Broida
130
Q

= pH 8.8, 340 nm, most commonly used

A
  1. Wacker method (forward/direct)
131
Q

= pH 7.2, 2x faster

A
  1. Wrobleuski LaDue (reverse/indirect)
132
Q

10-fold increase (LDH)

A

Hepatic carcinoma and toxic hepatitis

133
Q

2-3x URL

A

Viral hepatitis and cirrhosis

134
Q

Creatine Kinase Isoenzymes:

A

CK-BB
CK-MB
CK-MM

135
Q

= most anodal, brain

A

CK-BB

136
Q

= myocardium (20%)

A

CK-MB

137
Q

= least anodal, skeletal and smooth muscles (Major, 94-100%)

A

CK-MM

138
Q

Total CK: 50x URL (highest)

A

Duchenne’s muscular dystrophy

139
Q

Most specific indicator of myocardial damage (AMI)

A

CK-MB

140
Q

Not elevated in angina

A

CK-MB

141
Q

Methods (CK)

A
  1. Tanzer-Gilbarg (forward/direct) = pH 9.0, 340nm
  2. Oliver-Rosalki/ Rosalki & Hess (reverse/indirect) = most commonly used method, faster reaction; pH 6.8, 340nm
142
Q

= pH 9.0, 340nm

A
  1. Tanzer-Gilbarg (forward/direct)
143
Q

= most commonly used method, faster reaction; pH 6.8, 340nm

A
  1. Oliver-Rosalki/ Rosalki & Hess (reverse/indirect)
144
Q

Inside RBCs

A

Adenylate kinase

145
Q

Interferes w/ CK assay

A

Adenylate kinase

146
Q

Inhibited by adenosine monophosphate

A

Adenylate kinase

147
Q

Activate CK

A

N-acetylcysteine

148
Q

Do not contain CK

A

Liver cells and RBC

149
Q

Partially restore lost activity of CK

A

Cleland’s reagent and glutathione

150
Q

Reference method for CK

A

Electrophoresis

151
Q

CK relative index (CKI) (%) =

A

CK-MB/Total CK x 100

152
Q

Aldolase Isoenzymes:

A

Aldolase A = Skeletal muscles
Aldolase B = WBC, liver, kidney
Aldolase C = brain tissue

153
Q

= Skeletal muscles

A

Aldolase A

154
Q

= WBC, liver, kidney

A

Aldolase B

155
Q

= brain tissue

A

Aldolase C

156
Q

Marker for hepatobiliary diseases and infiltrative lesions of the liver

A

5’ Nucleotidase

157
Q

5’ Nucleotidase Methods:

A
  1. Dixon and Purdon
  2. Campbell, Belfield and Goldberg
158
Q

Located in the canaliculi of the hepatic cells

A

GGT

159
Q

Differentates the source of an elevated ALP level

A

GGT

160
Q

Sensitive indicator of occult alcoholism

A

GGT

161
Q

GGT Increased:

A

Obstructive jaundice
Alcoholic hepatitis (most sensitive)

162
Q

GGT Substrate:

A

gamma-glutamyl-p-nitroanilide

163
Q

Methods (GGT)

A
  1. Szass 2. Rosalki and Tarrow 3. Orlowski
164
Q

Monitor effects of relaxants (succinylcholine) after surgery

A

Cholinesterase/ Pseudocholinesterase

165
Q

Marker for organophosphate poisoning (Low CHS)

A

Cholinesterase/ Pseudocholinesterase

166
Q

Cholinesterase/ Pseudocholinesterase Methods:

A
  1. Ellman technic
  2. Potentiometric
167
Q

A.k.a. peptidyldipeptidase A or Kininase II

A

Angiotensin-Converting Enzyme

168
Q

Converts angiotensin I > angiotensin II (lungs)

A

Angiotensin-Converting Enzyme

169
Q

Indicator of neuronal dysfunction (Alzheimer’s disease – CSF)

A

Angiotensin-Converting Enzyme

170
Q

Ferrooxidase enzyme

A

Ceruloplasmin

171
Q

For hepatobiliary diseases

A

Ornithine carbamoyl transferase

172
Q

Drug induced hemolytic anemia (primaquine, antimalarial drug)

A

G-6-PD

Clinical Chemistry Review (15 decks)

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