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CLINICAL CHEMISTRY 2 > INTRODUCTION TO ENZYMOLOGY > Flashcards

INTRODUCTION TO ENZYMOLOGY Flashcards

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1
Q

Study of enzymes
1. Activity of enzymes
2. Chemical reactions it catalyzes
3. Clinical use

A

enzymology

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2
Q

Increases the speed of reaction

A

Protein catalysts

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2
Q

AKA excess energy

A

Activation Energy

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3
Q

The molecule upon which an
enzyme acts

A

substrate

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3
Q

Specific biologic proteins that
catalyze biochemical reactions

A

enzymes

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4
Q

Often water-free cavity. Region of an enzyme where substrate molecules bind and undergo chemical reaction

A

active site

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5
Q

changing the shape of the
enzyme or confirmation

A

Allosteric Site

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6
Q

impairs activity of the enzyme

A

Allosteric inhibitor

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7
Q

enhances activity of the enzyme

A

Allosteric activator

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8
Q

Results when an enzyme is
subject to posttranslational
modification

A

Isoform

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9
Q

Isoform of enzymes. Enzyme existing in different forms within the same individual but the same action

A

Isoenzyme

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10
Q

Organic cofactor such as nicotinamide adenine dinucleotide

A

Coenzyme

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10
Q

Inorganic cofactor like chloride
ion, magnesium ion

A

Activator

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11
Q

Nonprotein molecule that may
be necessary for enzyme activity

A

Cofactor

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12
Q

coenzyme that is bound tightly to the enzyme

A

Prosthetic group

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13
Q

Ability of an enzyme to choose
exact substrate from a group of
similar chemical molecules

A

Enzyme Specificity

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13
Q
  • Enzymes may recognize and catalyze
  • A single substrate
  • A group of similar substrates
  • A particular type of blood
A

Enzyme Specificity

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13
Q

AKA Zymogen
Inactive form or precursor of
enzyme

A

proenzyme

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14
Q

Oxidation and reduction

A

Oxidoreductase

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14
Q

– removal of H ion

A

Oxidation

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15
Q

– accept H ion

A

Reduction

16
Q

Addition of water to a bond resulting in bond breakage

A

Hydrolases

17
Q

Transfer of functional groups other than hydrogen from one
substrate to another

A

Transferases

18
Q

Catalyze the joining of two large molecules by forming a new chemical bond

A

Ligases

18
Q

Proposal that enzyme catalysis is a two-step process that consists of an initial adsorption whereby the substrate combines with the enzyme to form a noncovalent enzymesubstrate (ES) complex, followed by a second step in which
the ES complex decomposes into product (P) and free enzyme (E).

A

Michaelis-Menten Theory

19
Q

Catalyze removal of groups from substrates without hydrolysis; the product contains double bonds

A

Lyases

20
Q

Specific action of an enzyme with a single substrate postulated first by Emil Fischer in 1894

A

Lock and Key Theory

20
Q

Rearrange the functional groups within a molecule and catalyze the conversion of one isomer into another

A

Isomerase

21
Q

Concentration of substrates when the reaction reaches half of Vmax

A

Km

21
Q

Binding of a substrate or some other molecule to an enzyme
causes a change in the shape
of the enzyme resulting
enhancement or inhibition of
the enzyme’s activity

A

Induced Fit Theory

22
Q

Maximum velocity or rate at which the enzyme catalyzed a reaction

A

Vmax

23
Q

A double-reciprocal plot of the
Michaelis-Menten constant
which yields a straight line

A

Lineweaver-Burk Plot

24
Q

Reaction rate is directly proportional to the concentration of one of the reactants

A

First-order reaction

24
Q

temp for denaturation

A

40-50

25
Q

Reaction rate is independent of concentration of the reactants; increasing the concentrations of reactants does not speed up the rate of reaction

A

Zero-order reaction

25
Q

Reaction rate is directly proportional to the concentration of two reactants

A

Second-order reaction

26
Q

The higher the enzyme level, the
faster the reaction will proceed

A

Enzyme Concentration

26
Q

pH level of enzymatic reactions

A

7.0-8.0

26
Q

amylase denatures at what temp

A

45

27
Q

normal temp for er

A

37

27
Q

assay temp

A

25,30, or 37

27
Q

ck denatures at what temp

A

37

28
Q

it is able to fit at the active site. when it is there, the substrate is unable to bind to the enzyme and the desired reaction does not occur.

A

competitive inhibition

29
Q

bound to the regulatory site. the active site is thus changed, and the substrate can’t bind to the enzyme

A

noncompetitive inhibition

30
Q

Enzymatic reaction of interest is paired with a second enzymatic
reaction which can be conveniently and easily measured

A

Coupled-Enzyme Assay

31
Q

Reaction is stopped by denaturation using strong acid, strong base, detergent, heat, cold application, irreversible inhibitors, EDTA

A

Fixed-Time Method

32
Q

often convenient as a reagent for coupled-enzyme assay when neither NAD nor NADH is a coenzyme for the reaction

A

NAD or NADH

33
Q

Multiple measurements, usually of absorbance change, are made
during the reaction at specific time intervals usually every 30 secs of
60 secs, or continuously by continuous-recording
spectrophotometer

A

Continuous-Monitoring Method

33
Q

Amount of enzyme that will catalyze the reaction of 1 micromole of substrate per minute under specified conditions

A

International Unit

34
Q

Enzyme concentration

A

International Unit per Liter (IU/L)

35
Q

Amount of enzyme that will catalyze the reaction of 1 mole of
substrate per second under specified conditions

A

Katal Unit (mole/s)

CLINICAL CHEMISTRY 2 (9 decks)

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