Enzymes Flashcards

1
Q

a prosthetic group can never be composed of

A

amino acids

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2
Q

what are co-enzymes often derived from

A

vitamins

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3
Q

what is the difference between coenzymes and prosthetic groups

A

coenzymes are helper/partner molecules that bind loosely to the enzyme while prosthetic groups bind tightly to an enzyme

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4
Q

what enzyme was first isolated and what is it now known as

A

diastase now known as amylase

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5
Q

what name was first given to enzymes

A

ferments

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6
Q

how are proteolytic enzymes named and give an example

A

end with “in” for example trypsin

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7
Q

give an example of an enzyme that indicate the nature of the reaction without specifying the substrates

A

trans-carboxylase

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8
Q

what are the six primary classes of enzymes

A

oxidoreductases (EC1), transferases (EC2), hydrolases (EC3), lyases (EC4), isomerases (EC5), and ligases (EC6)

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9
Q

what new class of enzymes was added in 2018

A

translocases (EC7)

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10
Q

what is are the second digits of oxidoreductases

A

Second digit Hydrogen or electron donor
1 Alcohol ( >CHOH )
2 Aldehyde or ketone ( >C=O )
3 -CH = CH-
4 Primary amine ( -CHNH2 or -CHNH3 )
5 Secondary amine ( >CHNH- )
6 NADH or NADPH

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11
Q

what are the third digits of oxidoreductases

A

Third digit Hydrogen or electron acceptor
1 NAD+ or NADP+
2 Fe+³ ( e.g. cytochromes )
3 O2
99 An otherwise unclassified
acceptor

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12
Q

what are the second digits of transferases

A

Second digit Group transferred

 1                          1-carbon group
 2                          aldehyde or ketone group ( >C=O )
 3                          acyl group    (  –C–R )
                                                        ||
                                                       O
 4                          glycosyl ( carbohydrate ) group
 7                          phosphate  group
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13
Q

what are the third didgits of transferases

A

E.C. 2.1.1 : Enyzmes are methyltransferases (transfer –CH 3 )
E.C. 2.1.2 : Enyzmes are hydroxymethyltransferases
(transfer –CH 2OH )
E.C. 2.1.3 : Enyzmes are carboxyl- or carbamoyl-transferases

E.C. 2.4.1 : Enyzmes are hexosyltransferases (transfer hexose units)
E.C. 2.4.2 : Enyzmes are pentosyltransferases (transfer pentose units)

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14
Q

what is the exception of the third digit of tranferases

A

where there is transfer of phosphate groups: these cannot be described further, so there is opportunity to indicate the acceptor

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15
Q

give the digits of phosphate group transferases

A

E.C. 2.7.1 : Enzymes are phosphotransferases with an
alcohol group as acceptor
E.C. 2.7.2 : Enzymes are phosphotransferases with a
carboxyl group as acceptor
E.C. 2.7.3 : Enzymes are phosphotransferases with a
nitrogenous group as acceptor

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16
Q

what is the second digits of hydrolases

A

Second digit Bond hydrolysed

 1                  ester
 2                  glycosidic ( linking carbohydrate
                     units )
 4                  peptide  
 5                  C – N bonds other than peptides
17
Q

describe the third digits of hydrolases

A

E.C. 3.1.1 enzymes are carboxylic ester hydrolases
E.C. 3.1.2 enzymes are thiol ester hydrolases
E.C. 3.1.3 enzymes are phosphoric monoester
hydrolases
E.C. 3.1.4 enzymes are phosphoric diester hydrolases

18
Q

what are the second digits of lyases

A

Second digit Bond broken

 1                          C – C
 2                          C – O
 3                          C – N
 4                          C – S
19
Q

what are the third digits of lyases

A

Third digit Group removed

  1                       Carboxyl group ( CO2 )

  2                       Aldehyde group  ( –CH=O )

  3                       Ketoacid group ( –C.CO2 )
                                                         | |
                                                         O
20
Q

what is the second digit of isomerases

A

Second digit Type of reaction

1                                Racemization or epimerization

2                                Cis-trans izomerization

3                                Intramolecular oxidoreductases

4                                Intramolecular transfer reactions
21
Q

what are the third digits of isomerases

A

Third digit Substrate

1                     Amino acids

2                     Hydroxy acids

3                     Carbohydrates
22
Q

what are the second digits of ligases

A

Second digit Bond synthesized

1                              C — O
2                              C — S
3                              C — N
4                              C — C
23
Q

what are the third digits of ligases

A

The third digit further describes the bond being formed. Thus,
O
||
E.C. 6.3.1 enzymes are acid-ammonia ligases ( amide, —C —NH2 synthetases)
O
||
E.C. 6.3.2 enzymes are acid-amino ligases ( peptide, —C —N —, synthetases )

24
Q

what are the main classes of specificity of an enzyme

A
  1. absolute specificity
  2. group specificity (common functional group)
  3. Linkage specificity (particular type of chemical bond)
  4. stereospecificity (between D and L stereoisomers)
25
Q

true or false, catalysts effect equilibria

A

false

26
Q

what is the rate-limiting step

A

step in the overall reaction with the highest activation energy (highest-energy point in the diagram for interconversion of S and P)

27
Q

what equation is used to relate Keq and G

A

ΔG’° = -RT ln K’eq

28
Q

What is one I.U. defined as

A

as the amount of enzyme that can convert 1 micromole (μmol) of substrate into product per min at 25 ̊C

29
Q

what is specific activity

A

number of International Units of enzyme per milligram (mg) of protein. This term indicates the purity of the enzyme preparation

30
Q

what is the turnover number

A

amount of enzyme activity (in International Units) per mole of enzyme. tells how many substrate molecules are converted into products by each enzyme molecule

31
Q

at what temperature does enzymatic rates rise significantly

A

10 ̊C

32
Q

what is the pH rate for

a) pepsin
c) trypsin

A

a) 1-2

b) 7-8

33
Q

how does pH affect enzyme activity

A

Substrates can possess acidic or basic functional groups that also are affected by the pH solution. significantly influences the tertiary structure of the enzyme molecule and, thus, the activity of the enzyme

34
Q

where is glucose-6-phosphate found, and what is its optimum pH

A

in hepatocytes with optimum of 7.8

35
Q

what is Km

A

The substrate concentration that produces a velocity of 1/2 Vmax i.e. the Michaelis-Menten constant

36
Q

what happens to the Michaelis-Menten equation when the substrate concentration is very high

A

Michaelis-Menten equation reduces v ~ Vmax

37
Q

what cant increase the velocity of the reaction

A

increasing the substrate concentration

38
Q

what dies Km indicate

A

indicates the affinity of the substrate for the enzyme active site
small Km= strong affinity

39
Q

what happens when a phosphoryl group is added to Ser, Thr or Tyr residue

A

introduces a bulky, charged group into a region that was only moderately polar