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MLT 203 > Enzymes > Flashcards

Enzymes Flashcards

1
Q

enzyme definition

A

protein that catalyzes a biological reaction

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2
Q

not altered or consumed during reaction

  • reusable
  • accelerate reactions
A

enzymes

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3
Q

where are enzymes found?

A

in all body tissue

ex. heart attack = increased cardiac enzymes

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4
Q

clinical benefit of enzymes

A

helpful in making diagnosis

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5
Q

isoenzyme definition

A

enzymes that exist in multiple forms, but catalyze the same chemical reaction (same substrate)

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6
Q

how to differentiate isoenzymes

A

electrophoretic mobility
differences in absorption properties
reactions with specific antibodies

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7
Q

cofactor definition

A

non-protein molecules required for enzyme activation

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8
Q

cofactor types

A

Activators, Coenzymes

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9
Q

Common co-factor activators

A

Ca2+, Fe2+

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10
Q

common coenzymes

A

ATP, ADP, NAD

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11
Q

EDTA and calcium

A

some anticoagulants remove cofactors, EDTA removes calcium

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12
Q

Holoenzyme definition

A

Functional unit consisting of apoenzyme and cofactor

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13
Q

apoenzyme

A

protein portion of holoenzyme

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14
Q

Proenzyme/zymogen

A

inactive enzyme that requires biomechanical change to become active

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15
Q

Digestion enzymes

A

example of proenzyme

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16
Q

Cavity where substrate interacts

A

active site

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17
Q

site on enzyme where cofactors or regulatory molecules interact

A

allosteric site

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18
Q

Inhibitor attaches at

A

allosteric site

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19
Q

Basic enzyme reaction

A

S+E –> ES –> E+P

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20
Q

describes the nature of the reaction

ex. 1,4-glucagon-4-gluconohydrolase (amylase)

A

Systemic name

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21
Q

how do enzymes catalyze reactions?

A

lowering the activation rate

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22
Q

working/practical name

ex. amylase

A

recommended name

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23
Q

Numerical code

A 
first digit = class
second/third digit= subclass
fourth digit=specific serial number
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24
Q

Standard abbreviated name

A

accompanies recommended name

ex. AMS (amylase)

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25
Q

common abbreviated name

A

ex. AMY (amylase)

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26
Q

enzyme combines with only one substrate and catalyze one reaction

A

absolute specificity

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27
Q

enzymes combine with all substrates containing particular functional groups
ex. amino, phosphate, methyl groups

A

Group specificity

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28
Q

act upon certain chemical bonds

A

act upon certain chemical bonds

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29
Q

act upon specific stereoisomers of substrates.

ex. Glucose oxidase acts on D-glucose

A

Stereoisomeric specificity

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30
Q

excess energy that raises all molecules at a certain temperature to the activation energy
-determines how fast a reaction will proceed

A

activation energy

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31
Q

influencing factors on enzymatic reactions

A
  • substrate concentration
  • enzyme concentration
  • pH
  • temperature
  • cofactors
  • inhibitors
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32
Q

pH and enzymatic reactions

A

7.0-8.0 pH
changes can denature enzyme
buffer systems used to control pH

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33
Q

Temperature and enzymatic reactions

A

37 degrees C
increasing temp increases rate of reaction
extreme low/high can denature enzyme

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34
Q

reaction velocity and temperature

A

doubles for each 10 degree increase until 50 degrees then denaturation occurs

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35
Q

any substance that competes with the substrate for the active/binding sites (reversible)

A

competitive inhibition

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36
Q

a substance that binds to an allosteric site instead of competing with substrate

A

noncompetitive inhibition

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37
Q

relationship of the reaction velocity/rate to the substrate concentration

A

Michaelis-Menten (Km) Curve

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38
Q

Km constant

A

the substrate concentration in moles/liter when initial velocity is 1/2 V max

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39
Q

first-order kinetics

A

enzyme concentration is fixed, substrate is varies

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40
Q

rate is directly proportional to substrate concentration

A

first-order kinetics

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41
Q

method for measuring substrate

A

glucose

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42
Q

zero-order kinetics

A

reaction rate depends on enzyme concentration

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43
Q

plateau is reaches: all enzyme bound to substrate

A

zero-order kinetics

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44
Q

method for measuring enzyme

A

LD

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45
Q

low Km =

A

low substrate needed

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46
Q

high Km

A

more substrate is needed

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47
Q

clinical enzymes

A

measure activity of enzymes in patient serum

ex. LD, AST

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48
Q

substrate concentration should not be limiting factor (clinical enzymes)

A

need excess substrate and cofactors to handle possible abnormally high patient enzyme levels

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49
Q

if substrate and coenzyme are in excess, reaction rate is controlled by ENZYME

A

zero order kinetics in lab

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50
Q

measure amount of substrate in patient serum

A

analytical enzymes

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51
Q

glucose, cholesterol

A

analytical enzyme ex

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52
Q

analytical enzymes and kinetic order

A

first order kinetic

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53
Q

enzymes are not directly measured in lab

A

enzymes usually present in small quantities in bodily fluids, also difficult to isolate

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54
Q

how labs measure enzymes

A

-catalytic activity

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55
Q

enzymes activity can be tested by measuring

A

-increased product
-decreased substrate
-decreased coenzyme
-increased altered coenzyme
NAD+, NADH

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56
Q

leakage from cells (entry of enzymes)

A

damage to cell membrane

virus/chemical injury

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57
Q

altered production of enzymes

A

increased synthesis

increased osteoblastic activity

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58
Q

entry of enzymes into blood

A

leakage from cells

altered production of enzymes

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59
Q

clearance of enzymes

A

half life varies

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60
Q

increased serum levels of enzymes

A

cell damage,death
increased production
impaired disposition (jaundice/renal failure)

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61
Q

decreased serum enzymes

A

decreased formation (genetic or acquired)
enzyme inhibitor
lack of cofactors

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62
Q

measuring enzyme activity

A
  • single step reaction
    ex. NAD++Lactate -LD–> pyruvate + NADH

-consecutive enzyme reactions

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63
Q

product of one reaction becomes substrate of another reaction

A

consecutive enzyme reactions

64
Q

reaction is started and allowed to continue for a fixed period of time and the stopped. product is measured (enzyme activity)

A

fixed time

65
Q

multiple measurements of absorbance changes are made (enzyme activity)
-decreased substrate concentration/increased product

A

continuous monitoring/kinetic

66
Q

enzyme mass

A

measure protein mass NOT catalytic activity

ex. CK-MD isoenzymes

67
Q

clinical significance of enzyme testing

A

diagnosis of disease

68
Q

International unit of enzyme activity

A

1 umol substrate/ minute

IU/L

69
Q

Kata unit of enzyme

A

1 mole substrate/ 1 second

70
Q

Catalyzes transfer of phosphate between creatine and ATP

-rapid regeneration and storage of ATP

A

Creatine Kinase

71
Q

creatine kinase source

A

skeletal muscle
cardiac muscle
brain tissue

72
Q

CK Isoenzymes

A

CK-MM
CK-MB
CK-BB

73
Q

CK-MM location

A

striate muscle and serum

74
Q

Increased CK-MM

A

Myocardial Infarction, Dystrophy, polymyositis, hypothyroidism, IM injections

75
Q

CK-MB location

A

heart / skeletal muscle

76
Q

increased CK-MB

A

Myocardial infarction, angina, ischemia, cardiac surgery

77
Q

CK-BB location

A

brain, bladder, lung, prostate, uterus, colon, stomach, thyroid

78
Q

increased CK-BB

A

CNS, shock, seizure, carcinoma, placental/urterine trauma

79
Q

relative index equation

A

Relative index (RI)= (CK MB)/(total CK) X 100

80
Q

relative index ref range

A

<3% - normal

>6% = cardiac issue

81
Q

Relationship between thyroid and CK

A

Hypothyroid: Increased CL
Hyperthyroid: Decreased CK

82
Q

creatine kinase reference range

A

Male: 48-171 U/L
Female: 34-145 U/L

83
Q

Creatine kinase specimen

A

serum

84
Q

creatine kinase interferences

A 
adenylate kinase (hemolysis) -> false elevation 
CK is inactivated by light
85
Q

Oliver and Rosalki

A

common CK assay

86
Q

Lactate dehydrogenase (LD) source

A
  • skeletal muscle
  • cardiac muscle
  • liver
  • kidney
  • RBCs
87
Q

Catalyzes reversible reaction between pyruvate and lactate with NAD as a coenzyme

A

Lactate dehydrogenase

88
Q

LD-1

A

Cardiac, RBCs

89
Q

LD-2

A

Cardiac, RBCs

90
Q

LD-3

A

lung, pancreas

91
Q

LD-4

A

liver, kidney, placenta, pancreas

92
Q

LD-5

A

liver and skeletal muscle

93
Q

Healthy LD pattern

A

LD2>LD1>LD3>LD4>LD5

94
Q

MI: Flipped LD

A

LD1>LD2>LD3>LD4>LD5

95
Q

flipped LD pattern disease states

A

hematologic and neoplastic disorders
pernicious anemia
liver disease
heart prodlems

96
Q

LD assay specimen

A

serum

run asap and store at room temp

97
Q

LD reference range

A

125-220 U/L

98
Q

enzyme which reflect damage to hepatocytes

A 
Aspartate aminotransferase (AST)
Alanine aminotransferase (ALT)
99
Q

Enzymes which reflect cholestasis

A

Alkaline Phosphatase (ALP)

100
Q

Elevated in nearly all hepatobiliary disorders

high levels in biliary obstruction

A

Gamma-Glutamytransferase (GGT)

101
Q

Involved in transfer of amino group between aspartate and alpha-keto acids

A

AST (SGOT)

102
Q

enzyme elevated in acute hepatocellular disorders (ex. viral hepatitis, cirrhosis)

A

AST

103
Q

cholestasis

A

blockage downstream of liver (ex. pancreas, duodenum)

104
Q

Karmen method

A

couples reaction
malate dehydrogenase indicator
340 nm

105
Q

Karmen method enzyme

A

AST

106
Q

AST specimen

A

serum, heparin plasma
-centrifuged
stable at room temp 48 hrs

107
Q

AST ref range

A

5-35 U/L

108
Q

AST hemolysis

A

falsely elevates

AST is 10-15X higher in RBCs than serum

109
Q

transfers amino group from alanine to alpha-ketoglutarate to form glutamate nd pyruvate

A

ALT (SPGT)

110
Q

sources of ALT

A

liver
kidney
heart
skeletal muscle

111
Q

ALT specimen

A

serum/heparin plasma

centrifuged

111
Q

ALT specimen

A

serum/heparin plasma

centrifuged

112
Q

ALT reference range

A

7-45 U/L

113
Q

ALT enzyme assay

A

coupled reaction
lactate dehydrogenase indicator
340 nm

114
Q

AST>ALT

A

alcoholic liver issue

115
Q

nonspecific enzyme that frees inorganic phosphate from organic phosphate monoester which results in production of alcohol

A

Alkaline Phosphatase (ALP)

116
Q

Source of ALP

A

bone, liver, kidney, intestines, placenta, spleen

117
Q

elevated in bone activity, and paget’s disease

A

ALP

118
Q

ALP and liver disease

A

obstructive: 3-10X ULN (upper limit of normal)
hepatocellular: <3X ULN

119
Q

ALP and pregnancy

A

1.5X - 3X elevated

120
Q

ALP specimen

A

serum/heparin plasma

121
Q

ALP hemolysis

A

RBCs contain 6X more ALP than serum

122
Q

ALP ref range

A

teens: 54-369 U/L
males: 53-128 U/L
old men: 56-119 U/L
Females: 42-98 U/L
Old women: 53-141 U/L

123
Q

catalyzes phosphate esters, ph 5

A

Acid Phosphatase (ACP)

124
Q

Aids in detection of prostatic carcinoma
prostate conditions
forensic chemistry (rape)
elevated in bone disease

A

ACP

125
Q

ACP source

A

prostate, seminal fluid, bone, spleen, RBCs, platelets

126
Q

ACP specimen

A

serum/hep plasma

127
Q

ACP ref range (prostatic)

A

0-3.5 ng/mL

128
Q

Possible involved in peptide and protein synthesis, transport of amino acids and regulation of tissue glutathione levels

A

Gamma-Glutamyltransferase (GGT)

129
Q

GGT clinical signif

A

Indicator of liver damage

differentiating increased ALP–> GGT is not elevated in bone disease

130
Q

GGT specimen

A

serum/hep plasma

very stable

131
Q

GGT ref range

A

male: 6-55 U/L
female: 5-38 U/L

132
Q

Hepatits elevated enzymes

A

AST
ALY
GGT
Bilirubin

133
Q

Biliary obstruction elevated enzymes

A

ALP, GGT, Bilirubin

134
Q

digestive enzyme that catalyzes breakdown of starch and glycogen to carbohydrates

A

Amylase (AMY)

135
Q

AMY isoenzymes

A

P-AMY (pancreas)

S-Amy (Salivary)

136
Q

source of AMY

A

acinar cells of pancreas and salivary glands

137
Q

AMY acute pancreatitis

A

2.55x ULN

138
Q

AMY salivary gland lesions

A

mumps

parotitis

139
Q

increased amylase

A

peptic ulcer, appendicitis, cholecystitis, intestinal obstruction, ectopic pregnancy, macroamylsemia

140
Q

macroamylasemia

A

artifactual increase in serum amylase level

  • combines with immunoglobulins
  • UA amy decrease (complex too large to pass glomerulus)
141
Q

AMY assay

A

340 nm
Amyloclastic
Saccharogenic
Chromogenic

142
Q

Amylase Creatinine Clearance Ratio (ACCR)

A

acute pancreatitis >8%

macroamylasemia <2%

143
Q

amylase specimen

A

serum/hep plasma/urine

144
Q

amylase ref range

A

serum: 28-100 U/L
Urine: 1-15 U/h

145
Q

amylase errors

A

opiates increase levels

stabile

146
Q

Hydrolyzes triglycerides to produce alcohols and fatty acids

A

Lipase (LPS)

147
Q

LPS clinical sig

A 
Acute pancreatitis (more specific than amylase)
normal in salivary glands
148
Q

LPS assay

A

Cherry-Crandall
turbidimetry
550 nm

149
Q

LPS specimen

A

serum/hep plasma

150
Q

LPS ref range

A

<38 U/L

151
Q

LPS hemolysis

A

false decrease

152
Q

Acute pancreatitis

A

increased Amylase

increased Lipase

153
Q

Alolase

A

skeletal muscle diseases

154
Q

cholinesterase

A

pesticide poisoning

liver function test

155
Q

G-6-PD

A

RBCs
glucose metabolism
hemolytic anemia

MLT 203 (10 decks)

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