Module 1.3 (Enzymes) Flashcards

1
Q

_____ are key to life.
no ____ no life

A

enzymes

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2
Q

globular protein which functions as a biological catalyst, speeding up reaction rate by lowering activation energy without being affected by the reaction it catalyze

A

enzymes

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3
Q
  • are protein in nature (globular protein)
  • are composed of long chains of amino acids that have folded into a very specific three-dimensional shape which contains an active site.
A

enzymes

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4
Q

are RNA molecule with enzymatic activity

A

Ribozymes

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5
Q

Catalytic behaviour of any enzyme depends upon its _________________ (4)

A

primary, secondary, tertiary or quaternary structure

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6
Q

Enzymes of digestive tract and those found in blood are present in inactive form called ______or _______

A

zymogen or proenzymes.

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7
Q

is a region on the surface of an enzyme to which substrates will bind and catalyzes a chemical reaction.

A

active site

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8
Q

Enzymes are _________ for the type of the reaction they catalyze and for their substrate.

A

highly specific

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9
Q

Type of specificity recognized: (4)

A
  1. Absolute specificity
  2. group specificity
  3. reaction specificity
  4. stereospecificity
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10
Q

Enzymes with highest specificity and accuracy are involved in __________. These enzymes have proof reading function e.g. _________

A

copying and expression of genome;
DNA polymerase

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11
Q

Some enzyme require non protein molecule for their activity. So enzymes are conjugated proteins known as ________

A

holoenzyme

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12
Q

holoenzyme = _______ + _______

A

apoenzyme + cofactor/coenzyme

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13
Q

Enzyme without non protein part is inactive and called ______

A

apoenzyme

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14
Q

true or false

cofactors are inorganic compouns.

A

false

cofactors can be either inorganic or organic compounds.

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15
Q

The polymerization of deoxyribonucleotides into a DNA strand is catalyzed by_________, a holoenzyme. The catalytic activity of this enzyme is catalyzed by the ____________

A

DNA polymerase
magnesium ion

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16
Q

The enzymatic reactions takes place by binding of the substrate with the active site of the enzyme molecule by several ____ bonds

A

weak bonds

17
Q

is the first step in the enzyme catalyzed reaction

A

Formation of ES complex (enzyme-substrate complex)

18
Q

then ES complex is subsequently converted to _____ and _______

A

product
free enzyme

(E + S ‹——–› ES ——–› E + P)

19
Q

Two models of enzymes?

A

lock and key / template model
induced-fit model

20
Q

a model where the enzymes changes shape so its active site embraces the substrates

A

induced-fit model

21
Q

According to the IUBMB system of enzyme nomenclature enzymes are grouped into 6 major classe

A

EC 1 OXIDOREDUCTASES
EC 2 TRANSFERASES
EC 3 HYDROLASES
EC 4 LYASES
EC 5 ISOMERASES
EC 6 LIGASES

22
Q

Factors affecting reaction velocity of enzymes (8)

A

Temperature - dp, opt
Hydrogen ion concentration (pH) - dp, opt
Substrate concentration - dp
Enzyme concentration- dp
Products of the reaction- inhibit
Presence of activator/inhibitor
Allosteric effects
Time

23
Q

Rate of the reaction or velocity is _____ proportional to the Enzyme Concentration when sufficient substrate is present.

A

directly

24
Q

Accumulation of Product in a reaction causes _______ of enzyme activity.

A

inhibition

25
Q

Study of reaction rate and how they changes in response to change in experimental parameter is known as

A

kinetics

26
Q

Amount of _______ present is one of the key factor affecting the rate of reaction catalyzed by an enzyme in vitro

A

substrate

27
Q

The model involves one substrate molecule:

E + S ‹——-k1, k-1 ——› ES ——k2—— › E + P

K1 , k-1 and k2 are the rate constants

A

Michaelis- Menten Kinetics

28
Q

The mathematical equation that defines the quantitative relationship between the rate of an enzyme reaction and the substrate concentration is the

A

Michaelis-Menten equation:

V₀ = Vmax [S] / Km + [S]

V₀ is the observed velocity at the given [S]
Km is the Michaelis-Menten constant
Km = (K-1 + K2) / K1
Vmax is the maximum velocity at saturating [S]
conc.

29
Q

A linear representation is more accurate and convenient for determining Vmax and Km.

is obtained by taking reciprocal of both the side of Michelis-Menton equation.

A

Lineweaver-Burk (double reciprocal) plot

30
Q
  • Any substance that can diminish the velocity of an enzyme catalyzed
  • These include drugs, antibiotics, poisons, and anti-metabolites.
  • Useful in understanding the sequence of enzyme catalyzed reactions, metabolic regulation, studying the mechanism of cell toxicity produced by toxicants.
  • Forms the basis of drug designing.
A

Enzyme Inhibiton

31
Q

Types of Enzyme Inhibiton (2)

A
  • Reversible inhibitors
  • Irreversible inhibitors
32
Q

Reversible inhibitors can be classified into : (3)

A
  • Competitive
  • Non-competitive
  • Un-competitive
33
Q

Binds only to the enzyme-substrate
complex.

Does not have the capacity to bind to the free enzyme.

Not overcome by increasing substrate concentration.

Both the Km and Vmax are reduced.

A

Un-competitive Inhibiton