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CCHM 2 > LEC1 - CCHM > Flashcards

LEC1 - CCHM Flashcards

1
Q

biologic proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition

A

ENZYMES

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2
Q

e same catalytic function but may differ in select physical properties, such as electrophoretic mobility,
solubility, or resistance to inactivation

is generally used when discussing
such forms of the enzymes, although the International Union of Biochemistry (IUB) suggests
restricting this term to multiple forms of similar genetic origin

A

isoenzyme

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3
Q

An +_____ results when an
enzyme is subject to posttranslational modifications with a functional group added to an amino
acid. Isoenzymes and isoforms contribute to heterogeneity in properties and function of
enzymes because these measured properties are influenced by changes in amino acid
chemistry and the resulting changes in structural features.

A

isoform

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4
Q

classification of practical or trivial names of enzyme

A

According to the name of the substrate with the addition of the suffix “ase”

According to the type of reaction they catalyzed.

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5
Q

Transfer of amino group from substrate to another - ____

A

transferase

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6
Q

Transfer to phosphate group from a high energy phosphate compound to its substrate - _____

A

kinase

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7
Q

Effect of hydrolysis on phosphate esters – ___

A

phosphatase

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8
Q

Removal of hydrogen atoms from its substrate - ____

A

dehydrogenase

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9
Q

systematic name is According to the numerical designation given by the ____

A

Enzyme Commission (E.C.)

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10
Q

Systematic name for lactate dehydrogenase

A

E. C. 1. 1. 1. 27

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11
Q

systematic name for amylase

A

E. C. 3. 2. 1 .1

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12
Q

systematic name for alanine aminotransferase

A

E. C. 2. 6.1. 2

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13
Q

removal or addition of electrons (reduction-oxidation [“redox”] reaction.

A

Oxidoreductases

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13
Q

systemic name

discuss how the numbers are given

A

1st - class
2-3rd - subclass
4th- serial number

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14
Q

classification of Oxidoreductases

A

oxidase
dehydrogenase

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15
Q

example of oxidase

A

cytochrome oxidase

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16
Q

example of dehydrogenase

A

lactate dehydrogenase (LDH)
malate dehydrogenase (MDH)
isocitrate dehydrogenase (ICD)

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17
Q
  • catalyze the transfer of a chemical group other than hydrogen from one substrate to another
A

Transferase

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18
Q

examples of transferase

A

(a) aspartate aminotransferase (AST)
(b) alanine aminotransferase (ALT)
(c) creatine kinase (CN) or
creatine phosphokinase (CPK)
(d) gamma-glutamyl transferase (GGT)
(e) ornithine carbamyl transferase (OCT)

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19
Q
  • hydrolyze the splitting of a bond by the addition of water (hydrolysis reaction
A

Hydrolase

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20
Q

classification of hydrolase

A

esterases
peptidases
glycosidase

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21
Q

examples of esterases

A

acid phosphatase (ACP)
alkaline phosphatase (ALP)
cholinesterase (CLS)
lipase (LPS)

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22
Q

example of peptidase

A

trypsin (PTS)
pepsin (PPS)
leucine aminopeptidase (LAP)

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23
Q

example of glycosidase

A

amylase (AMS)
amylo 1,6 glycosidase
galactosidases

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24
Q

remove groups from substrate without hydrolysis, leaving only double bonds in the molecular structure of the product.

A

Lyases

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25
Q

examples of Lyases

A

(a) aldolases
(b) glutamate decarboxylase
(c) pyruvate decarboxyiase
(d) tryptophan decarboxylase

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26
Q

catalyzes the interconversion of geometric, optical or positional isomers of the substrate compound

A

isomerases

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27
Q

examples of isomerases

A

(a) glucose phosphate isomerase
(b) ribose phosphate lsomerase

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28
Q
  • joins two substrate molecules together using the energy released from hydrolyzing a pyrophosphate bond to a high-energy phosphate compound.
A

Ligases (Synthetases)

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29
Q

ligases is Coupled with breaking the ___ bond in ATP

A

pyrophosphate

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30
Q

example of ligases (synthetases)

A

Glutathione synthetase

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31
Q

an active substance formed by combination of a coenzyme (cofactor) and apoenzyme.

A

holoenzyme

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32
Q

formula for holoenzyme

A

cofactor X apoenzyme

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33
Q

the protein portion subject to denaturation, in which the enzyme loses its activity.

A

apo enzyme

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34
Q

Catalytically inactive protein when cofactor is removed

A

apoenzyme

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35
Q

are apo enzyme heat labile and dialyzable.

A

yes

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36
Q

enzymes present in an individual with similar enzymatic activity but differ in their physical biochemical and immunologic characteristics

A

isoenzyme

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37
Q
  • enzyme whose metal ions are intrinsically part of the molecule such as catalases and cytochrome oxidase
A

Metalloenzyme

38
Q

inactive precursor of enzymes,

A

proenzyme

39
Q

proenzyme are also referred to as ___

A

zymogens

40
Q

substances acted upon by the enzymes which are specific for each of their particular enzyme.

A

Substrates

41
Q

these are non-protein substance/compounds needed by an enzyme before enzymatic activity can be manifested. ____ are thermostable and dialyzable

A

Cofactors

42
Q

the cofactor in Organic molecule act as ___.

A

Coenzyme

43
Q

It hastens enzymatic reaction but undergoes a change or is consumed to another product

A

cofactor

44
Q

examples of co factor

A

NAD – nicotinamide Adenine dinucleotide
NADP - nicotinamide Adenine dinucleotide phosphate

45
Q

the cofactor in Metal ion as an ___

A

Activator

46
Q

a cofactor in metal ion - activator

In such, the metal ion may serve as:

A

a bridge to hold the substrate and enzyme together

the primary catalytic center

stabilizing agent In the conformation for catalytic activity.

47
Q

An enzyme (E) catalyses a reaction by combining with its substrate (S) to create an ______

A

enzyme—substrate complex (ES)

48
Q

The enzyme-substrate complex according to _____ can either dissociate back to E + S or breakdown to product (P) and free enzyme (provided that the product has a low affinity for the enzyme).

A

Michaelis and Menten

49
Q

THE _____ GIVES THE MEANS TO DETERMINE TOTAL ENZYME CONCENTRATION IN SERUM AND OTHER BODY FLUIDS

A

MICHAELIS-MENTEN EQUATION

50
Q

Accurately describes virtually all single-substrate enzyme-catalyzed reactions and many bisubstrate reactions in which the concentration of one substrate is constant throughout the course of the reaction.

A

Michaelis-Menten Equation

51
Q

Types of Specificity

A

absolute
group
bond
stereoisomeric

52
Q

a type of specificity in which the enzymes combine with only one substrate and catalyzes only one corresponding reaction

A

absolute specificity

53
Q

a type of specificity in which the enzymes combining with all substrates containing a particular chemical group

A

group enzymes

54
Q

a type of specificity in which enzymes are specific to chemical bonds

A

bond specificity

55
Q

a type of specificity in which enzymes are predominantly combined with only one optical isomer of a certain compound

A

stereoisomeric specificity

56
Q

____’s LOCK and KEY THEORY

A

Emil Fischer

57
Q

It is based on the rigid enzyme molecule into which the substrate fits. The shape of the key (substrate) must conform into the lock (enzyme).

A

Emil Fischer’s LOCK and KEY THEORY

58
Q

It is based on the attachment of a substrate to the active site of an enzyme, which then causes conformational changes in the enzyme

A

Koshland’s INDUCED FIT THEORY

59
Q

This theory Is more acceptable because the protein molecule Is flexible enough to allow conformational changes and also allow some explanation on the influence of hormones on enzymatic activity.

A

Koshland’s INDUCED FIT THEORY

60
Q

This phenomenon states that a certain enzyme has the ability to adapt to their biochemical systems

A

enzyme induction

61
Q

Factors Affecting Enzyme Reactions:

A

enzyme concentration
substrate concentration
temperature
hydrogen ion concentration or pH

62
Q

An increase in the concentration of enzyme produces an increase in the rate of reaction, provided that the other conditions remain the same and that a constant but excess amount of substrate Is present

A

enzyme concentration

63
Q

Temperature - The rate of any chemical reaction is usually increased 2-3 times for every _______degrees Celsius rise in temperature

A

I0* C

64
Q

Enzymatic reactions proceed at their fastest rate at an optimum pH and are considerably slowed or even stopped at higher or lower pH values

A

Hydrogen Ion Concentration or pH

65
Q

Types of Reaction Order:

A

Zero Order Reaction
First Order Reaction

66
Q

reaction order

is the rate of reaction linear with time, independent of concentration of substrate and directly proportional to enzyme concentration.

A

Zero Order Reaction

67
Q

reaction order

the rate of reaction is determined by the concentration of substrate as well as of enzymes (the rate of reaction changes continuously with time as the substrate is consumed

A

First Order Reaction

68
Q
  • These are substances that compete with the substrate for enzyme binding because they are chemically analogous to the substrate and bind to the active sites of enzymes
A

Competitive Inhibitor

69
Q

These are substances that do not resemble the substrate and bind to the enzyme in areas other than the active site

A

Non- competitive Inhibitor

70
Q

inhibits enzyme by binding to the enzyme-substrate complex

A

Uncompetitive Inhibition

71
Q

– has the ability to bind to either only the enzyme or the ES complex at a different site from the substrate active site

A

Mixed Inhibitor

72
Q

MEANS OF MEASURING ENZYME ACTIVITY

A

Change in Coenzyme Concentration
Increase in Product Concentration
Decrease in Substrate Concentration

73
Q

Types of Enzyme Assays

A

Endpoint Analysis
Multi-point and Kinetic Assay
Use of Coupled Reactions

74
Q

a type of enzyme assay which the Reaction is initiated by addition of substrate

A

Endpoint Analysis

75
Q

a type of enzyme assay which the Reaction is allowed to proceed for a period of time

A

Endpoint Analysis

76
Q

a type of enzyme assay which the Measurement is done at the end of the react

A

Endpoint Analysis

77
Q

Endpoint Analysis disadvantage

A

underestimation of the “true” enzyme activity and linearity of reaction cannot be observed

78
Q

a type of enzyme assay that is about the Change in concentration of the indicator substance at several intervals

A

Multi-point and Kinetic Assay

79
Q

a type of enzyme assay that is about the Continuous measurement of change in concentration as function of time

A

Multi-point and Kinetic Assay

80
Q

a type of enzyme assays in which Enzymatic activity is measured by coupling the activity with colorimetric reaction

A

Use of Coupled Reactions

81
Q

UNITS FOR EXPRESSING ENZYME ACTIVITY

A

International Unit (I.U. or U)
Katal Unit (K.U.)

82
Q

Equivalent to the amount of enzyme that catalyzes the conversion of 1 micromole of substrate per minute under controlled conditions.

A

International Unit (I.U. or U)

83
Q

Equivalent to the amount of enzyme that catalyzes the conversion of 1 mole of substrate per second under controlled conditions

A

Katal Unit (K.U.)

84
Q

1.0 IU = _____nkat

A

17

85
Q

PITFALLS IN ENZYME ASSAYS

Hemolysis cause falsely _____ values due to the release of enzymes from red blood cells.

A

elevated

86
Q

PITFALLS IN ENZYME ASSAYS

is the preferred specimen due to the adverse effects of anticoagulants on enzyme activity.

A

Serum

87
Q

PITFALLS IN ENZYME ASSAYS

Lactescent or milky serum causes variable ___ by the spectrophotometer.

A

absorption

88
Q

PITFALLS IN ENZYME ASSAYS aside from hemolysis, use of serum, and lactescent or milky serum

A

storage ad presence of inhibitors

88
Q
A
89
Q

Storage of Samples

Most enzymes are stable at ____ for at least 24 hrs

A

6*C

90
Q

storage of samples

Few enzymes are ___ at refrigerator temp (LD 4 and 5)

A

inactivated

91
Q

Quality Control Program for Enzyme Assays

A
  1. Strict adherence to zero-order kinetics
  2. Proportionality with increments of sample
  3. Use of pooled frozen serum or stable reference materials as controls
  4. Replicate measurements to evaluate precision of assays

CCHM 2 (7 decks)

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