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Clinical Chemistry II > CC2 Enzymes - Feb 26 quiz > Flashcards

CC2 Enzymes - Feb 26 quiz Flashcards

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1
Q

6 Enzyme Classes

A

Class 1 Oxidoreductases
Class 2 Transferases
Class 3 Hydrolases
Class 4 Lyases
Class 5 Isomerases
Class 6 Ligases

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2
Q

ENZYME NOMENCLATURE consisting of 4 numbers separated by periods

A

Enzyme class
subclass
Sub-subclass
Serial number for substrate

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3
Q

Enzymes follow the ___ kinetics

A

Michaelis-Menten

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4
Q

Enzymes undergo function as governed by two theories

A

Fischer’s Lock and Key theory
Koshland’s Induced Fit theory

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5
Q

theory….enzyme (lock) and substrate (key) perfectly fits

A

Fischer’s Lock and Key theory

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6
Q

theory ….enzyme undergoes conformational changes to accommodate shape of the substrate

A

Koshland’s Induced Fit theory

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7
Q

factors affecting enzymes (7)

A

substrate concentration,
enzyme concentration,
pH,
temperature,
cofactors,
inhibitors

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8
Q

Types of Enzyme Assay (3)

A

● Endpoint Analysis
● Multipoint Assay
● Kinetic Assay

✅● Endpoint Analysis
= reaction is initiated by the addition of substrate
and allowed to proceed for a period of time
= measurement of the product or substrate is done at the end of the reaction
✅ ● Multipoint Assay
= measures the change in concentration of the substance at several intervals during the course of the assay
✅ ● Kinetic Assay
= continuous measurement of change in concentration as a function of time

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9
Q

ENZYME INHIBITION (4)

A

✅No inhibition – Absence of inhibitor
✅Competitive – inhibitor binds to ACTIVE SITE
✅Noncompetitive – inhibitor binds to ALLOSTERIC SITE
✅Uncompetitive– inhibitor binds to E-S COMPLEX

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10
Q

interpret… CK-MB present and LD

A

both MI and non MI cases

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11
Q

interpret… CK-MB present and flipped LD

A

100% predictive value that there is MI

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12
Q

(4) Pronounced elevation of CK (5 or more times normal)

A

● Duchenne’s muscular dystrophy
● polymyositis
● dermatomyositis
● AMI

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13
Q

Mild or moderate elevation (2-4 times Normal)

A

● severe exercise, trauma, surgical procedure, IM injections
● delirium tremens, alcoholic myopathy
● MI, severe iochemic injury
● pulmonary infarction
● pulmonary edema
● hypothyroidism
● acute agitated psychoses

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14
Q

Reversible conversion of lactate to pyruvate using NAD+ as cofactor

A

LACTATE DEHYDROGENASE

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15
Q

LD class heart, brain, RBC

A

LD1 and LD2

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16
Q

LD class brain kidney lung

A

LD3

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17
Q

LD class liver, skeletal muscle, kidney

A

LD4 and LD5

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18
Q

LD Pronounced Elevation (5 or more times Normal)

A

● Megaloblastic anemia
● Widespread carcinomatosis, esp. hepatic metastases
● Septic shock and hypoxia
● Hepatitis
● Renal infarction
● Thrombotic thrombocytompenic purpura

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19
Q

LD Moderate Elevation (3-5 times Normal)

A

● MI
● Pulmonary infarction
● Hemolytic conditions
● Leukemia
● IM
● Delirium tremens
——- (a psychotic condition typical of withdrawal in chronic alcoholics, involving tremors, hallucinations, anxiety, and disorientation)

● Muscular dystrophy

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20
Q

LD Slight Elevation (Up to 3 times Normal)

A

● Most liver diseases
● Nephrotic syndrome ● Hypothyroidism
● Cholongitis

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21
Q

NOTE : Association of LD1 & LD2 is useful in confirming diagnosis
of MI after CK has returned to normal (LD flipped) Note: hemolysis should be absent

A

NOTE : Association of LD1 & LD2 is useful in confirming diagnosis of MI after CK has returned to normal (LD flipped) Note: hemolysis should be absent

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22
Q

● first protein marker to diffuse out of ischemic muscle cells

● presumptive for AMI (not specific, only sensitive)

A

MYOGLOBIN

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23
Q

troponin polypeptides … released into circulation following myocardial injury (highly specific)

A

I & T released into circulation following myocardial injury (highly specific)

✅ skeletal muscles have different troponins
✅ peaks at 4-8 hours; fresh appearance in serum suggests AMI

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24
Q

● Act on compounds with single PO4 groups
● has orthophosphate ester monohydrolase activity
● optimally active at pH 5 (acid phosphatase) most active at pH 9 (alkaline phosphatase)

A

PHOSPHATASES

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25
Q

major enzyme in detecting prostatic cancer

A

Prostatic ACP

✅ medicolegal evaluation of rape- vaginal swab during pelvic exam; replaced DNA testing

26
Q

● high in bone, liver, intestine, kidney, WBCs & placenta

● Placenta ● intestine
● germ cell & lung
● bone, liver, kidney, granulocytes

A

ALP

27
Q

most common method of distinguishing ALP isoenzymes

A

heat fractionation

✅ (serum heated at 56OC for 15 min. & assayed for remaining ALP activity)

28
Q

Bone ALP elevation in cases of

A

osteoblastic growth responses,
healing bones,
Paget’s disease,
bone CA,
myeloma,
rickets,
hyperparathyroidism
osteomalacia

29
Q

The placenta oncofetal form of ALP

A

✅ Regan isoenzyme

30
Q

blood type ___ and ____secretory status- secrete intestinal ALP into circulation after a meal

A

O & B

31
Q

specific marker released from lymphocytes during HIV infection in children

A

ALP (band 10)-

32
Q

ALP Pronounced elevations (5 or more time Normal)

A

Bile duct obstruction (intrahepatic or extra)
Biliary cirrhosis
Paget’s disease
Osteogenic sarcoma Hyperparathyroidism

✅Moderate elevation (3-5 times Normal)
Granulomatous or infiltration dses of liver
IM
Metastatic tumor in bone
Metabolic bone disease (rickets, osteomalacia)

✅ Slight elevation (up to 3 times Normal)
Viral hepatitis
Cirrhosis (intestinal isoenzyme often present Healing fractures
Pregnancy (placental isoenzyme) Normal growth patterns in children

33
Q

CONDITIONS IN WHICH THE SERUM ALP IS INCREASED (5)

A

Healing fractures
Biliary cirrhosis
Rickets
Osteoporosis
Bone cancer

34
Q

Enzyme that finds out the severity of inflammatory muscle dx….

Glycolytic enzyme that splits fructose- 1,6 diphosphate into two triose phosphate molecules in the metabolism of glucose

A

ALDOLASE

35
Q

Catalyze the reversible transfer of an amino group between an amino acid and an alpha-keto acid

A

AMINOTRANSFERASES

36
Q

2 AMINOTRANSFERASES

A

ALT
AST

37
Q

large amount in liver, myocardium & skeletal
muscle; moderate in RBCs

A

AST

38
Q

specimens for amylase

A

Urine
Serum
Saliva
Pleural fluid
Peritoneal fluid

✅diastase
✅ found in salivary glands & pancreas

39
Q

Insecticide poisoning & Nephrotic syndrome

A

CHOLINESTERASE

39
Q

Note:
ANGIOTENSIN-CONVERTING ENZYME
: bp regulation

Produced in the lungs by macrophages & epithelioid cells

✅ Primary diagnostic use is for active sarcoidosis

✅ used to evaluate active granulomatous pulmonary dse

A

ANGIOTENSIN-CONVERTING ENZYME

40
Q

GGT clinical significance

A

✅ obstructive jaundice
✅ metastatic liver cancer
✅ intrahepatic cholestasis

41
Q

discuss how to differentiate Bone and Liver cancer using GGT and ALP…..which enzyme is elevated?

A

-

42
Q

Lysozyme/Muramidase elevated in

A

**In serum:
**✅ Acute monocytic leukemia
✅ Acute myelomonocytic leukemia

**found in
**✅ tears
✅ saliva
✅ sputum
✅ also granulocytes & monocytes

43
Q

📝

A

Liver————– AST
Heart ———— CK-MB
Skeletal Muscle ———CK-MM
Bone ——- ALP (heat labile)
Prostate ———– ACP
Pancreas ———— AMS
Brain ————– CK-BB

44
Q

specificity of enzymes

A

Absolute
Bond
Group
Stereospecificity

45
Q

features of coenzymes

A
  • Transfer a functional group
  • Essential for enzyme activity
  • Heat stable low MW organic substance
  • Combines loosely with apoenzyme
  • Can be separated from apoenzyme via dialysis
46
Q

Factors that affect enzymatic activity

A
  • [H*]
  • Activators
  • Inhibitors
  • Enzyme concentration
  • Substrate concentration
47
Q

Enzymes composed wholly of protein are known as

A

simple enzymes

48
Q

enzymes which are composed of protein plus a relatively small organic molecule.

A

complex enzymes aka Holoenzymes

49
Q

the protein component of enzyme…. while the non protein??

A

apoenzyme
Coenzyme or prosthetic group (non protein)

50
Q

four possible mechanisms of catalysis

A
  1. Catalysis b yBond Strain
  2. Catalysis by Proximity and Orientation
  3. Catalysis Involving Proton Donors (Acids) and Acceptors (Bases)
  4. Covalent Catalysis
51
Q

Draw the Fischer’s Lock & Key Model

A

….

52
Q

Changes in pH &temperature affect the…

A

Tertiary structure
Noncovalent forces

53
Q

change their structure in response to binding of effectors.

A

Allosteric enzymes

54
Q

Thiamine coenzyme

A

TPP

55
Q

Riboflavin coenzyme

A

FMN, FAD

56
Q

Competitive inhibitors bind reversibly to the enzyme, preventing the binding of substrate. On the other hand, binding of substrate prevents binding of the inhibitor. Substrate and inhibitor compete for the enzyme.

A

Competitive inhibition

57
Q

In uncompetitive inhibition the inhibitor can not bind to the free enzyme, but only to the ES-complex.

A

Uncompetitive inhibition

58
Q

Non-competitive inhibitors can bind to the enzyme at the same time as the substrate, i.e. they never bind to the active site.

A

Non-competitive inhibition

59
Q

This type of inhibition resembles the non- competitive, except that the EIS-complex has residual enzymatic activity.

A

Mixed inhibition

60
Q

🫴🐈

A

✅ Competitive Inhibitor
* Specifically at the catalytic site, where it competes with substrate for binding in a dynamic equilibrium- like process.
* Inhibition is reversible by substrate.
* Vmax is unchanged; Km, as defined by [S] required for 1/2 maximal activity, is increased.
✅ Noncompetitive Inhibitor
* Binds E or ES complex other than at the catalytic site. Substrate binding unaltered, but ESI complex cannot form products.
* Inhibition cannot be reversed by substrate
* Km appears unaltered; Vmax is decreased proportionately to inhibitor concentration.
✅ Uncompetitive Inhibitor
Binds only to ES complexes at locations other than the catalytic site.
* Substrate binding modifies enzyme structure, making inhibitor- binding site available.
* Inhibition cannot be reversed by substrate.
* Apparent Vmax decreased; Km, as defined by [S] required for 1/2 maximal activity, is decreased.Note

Clinical Chemistry II (7 decks)

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