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biochem lec > enzymes p2 nucleotides 1,2 finals > Flashcards

enzymes p2 nucleotides 1,2 finals Flashcards

1
Q

three types of specificity enzymes

A

stereochemical, reaction, substrate

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2
Q

only one of the isomers which acts as a substrate for an enzyme action

A

optical specificity

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3
Q

specific to only one isomer even if the compound is one type of molecule

A

stereospecificity

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4
Q

one enzyme can catalyze only one of the various reactions

A

reaction specificity

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5
Q

one enzyme catalyzes or acts on only one substrate

A

absolute specificity

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6
Q

enzymes that catalyze similar molecules with the same functional group (trypsin and chymotrypsin)

A

group specificity

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7
Q

observed in proteolytic enzymes, glycosidases, and lipases which act on peptite bonds, glycosidic bonds and ester bonds

A

bond specificity

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8
Q

enzyme is most active on its optimum temperature

A

effect of temperature

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9
Q

enzymatic reaction depends on the pH of the medium

A

effect of pH

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10
Q

enzymatic reaction is directly proportional to the enzyme concentration

A

effect of enzyme concentration

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11
Q

products formed as a result of enzymatic reaction may accumulate, and this excess of product may lower the enzymatic reaction by occupying the active site of the enzyme.

A

effect of product concentration

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12
Q

reaction is directly proportional to the substrate concentration, but only true up to a certain concentration after which the increasing concentration of substrate does not further increase the velocity of the reaction

A

effect of substrate concentration

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13
Q

Certain enzymes is dependent on metal ion activators and coenzymes

A

effect of activators and coenzyme

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14
Q

Whenever the active site is not available for binding of the substrate, the enzyme activity may be reduced.

A

effect of modulators and inhibitors

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15
Q

Time required for completion of an enzyme reaction increases with decreasing temperature from its optimum.

A

effect of time

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16
Q

the lock is the enzyme and the key is the substrate. Only the correctly sized key (substrate) fits into the key hole (active site) of the lock (enzyme

A

lock-and-key model

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17
Q

he postulated the lock-and-key model in 1894

A

Emil Fischer

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18
Q

the substrate plays a role in determining the final shape of the enzyme and that the enzyme is partially flexible.

A

induced fit model

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19
Q

he created the induced fit model in 1958

A

Daniel E. Koshland, Jr.

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20
Q

These enzymes contains active sites with catalytic residues that can form temporary covalent bonds with the substrate molecules.

A

covalent catalysis

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21
Q

These implies that for the reaction to occur, they must be close enough and must also have the proper orientation.

A

catalysis by proximity and orientation

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22
Q

Active sites may contain residue such as histidine that can participate in hydrogen ion transfer.

A

acid-base catalysis

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23
Q

Metal atoms such as Zinc, Magnesium and Iron are used as cofactors by a multitude of different enzymes.

A

metal-ion catalysis

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24
Q

Rates of enzyme-catalyzed reactions can be decreased by a group of substances called inhibitors.

A

enzyme inhibition

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25
Q

is a substance that slows or stops the normal catalytic function of an enzyme by binding to it

A

enzyme inhibitor

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26
Q

is a molecule that sufficiently resembles an enzyme substrate in shape and charge distribution that it can compete with the substrate for occupancy of the enzyme’s active site

A

competitive enzyme inhibitor

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27
Q

When a competitive inhibitor binds to the enzyme active site, inhibitor remains unchanged (no reaction occurs), but its physical presence at the site prevents a normal substrate molecule from occupying the site – result is decrease in enzyme activity.

A

reversible competitive inhibition

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28
Q

is a molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site

A

noncompetitive enzyme inhibitor

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29
Q

substrate can still occupy the active site, but the presence of the inhibitor causes a change in the structure of the enzyme sufficient to prevent the catalytic groups at the active site from properly effecting their catalyzing action

A

reversible noncompetitive inhibition

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30
Q

Occurs when (II) binds only to the enzyme- substrate complex (ESES) and not free EE.

A

uncompetitive inhibition

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31
Q

is a molecule that inactivates enzymes by forming a strong covalent bond to an amino acid side-chain group at the enzyme’s active site

A

irreversible enzyme inhibitor

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32
Q

inhibitors do not have structures similar to that of enzyme’s normal substrate

A

irreversible inhibition

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33
Q

It is often regulated by the cell. Often the reason for this is to conserve energy because if the cell runs out of chemical energy, it will die; therefore many mechanism exist to converse energy.

A

regulation of the enzyme activity

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34
Q

Enzymes that have more than one a single site. It has an active sites that can be altered by binding of a small molecules called effector molecules or regulators.

A

allosteric enzymes

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35
Q

inhibit enzyme action

A

negative allosterism

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36
Q

stimulate enzyme action

A

positive allosterism

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37
Q

The production of the enzyme in an active form.

A

proenzyme

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38
Q

This is a process in which a chemical group is covalently added to or removed from the protein.

A

protein modification

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39
Q

It is an enzyme regulation process in which formation of a product inhibits an earlier reaction in the sequence.

A

feedback control

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40
Q

refers to the enzymes that are used directly or as components of the assay system for the determination of number of substances

A

diagnostic enzymes

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41
Q

is the component that is neither a blood cell (serum does not contain white or red blood cells) nor a clotting factor; it is the blood plasma with the fibrinogens removed.

A

serum

42
Q

➜ Important enzyme found throughout the body and involved in glucose metabolism
➜ The analysis of isoenzyme patterns can help in the investigation of myocardial infarction.
➜ Tetramer of 2 different subunits(H or M)

A

lactate dehydrogenase

43
Q

is found predominantly in heart muscle, kidney and in RBCs

A

LDH1 and LDH2

44
Q

is found in a variety of tissues such as spleen, lung, endocrine glands and lymph nodes

A

LDH3

45
Q

found in liver, skin and skeletal muscle is the least stable and runs the shortest on electrophoresis

A

LDH4 and LDH5

46
Q

o Formally known as glutamate pyruvate transaminase (GPT)
o Found in high concentrations in liver cells and in much smaller concentrations elsewhere.

A

alanine transaminase

47
Q

➜ High levels are found in liver, bone, placenta and intestine
➜ Used as a marker of cholestatic liver disease
➜ Separation by electrophoresis and also assessed using inhibitors, specific substrates or by heat
inactivation of other isoenzymes.

A

alkaline phosphatase

48
Q

➜ Also known as creatine phosphatase (CPK)
➜ Mainly found in heart and skeletal muscle and
in brain

A

creatine kinase

49
Q

➜ Maximum activity-pH-5-6
➜ Found in large amounts in prostate glands and its assay in plasma has been used in the diagnosis of prostatic carcinoma

A

acid phosphatase

50
Q

➜ The enzyme catalyze the hydrolysis of choline esters
➜ Presence is assumed when the muscle relaxant scoline is administered.

A

cholinesterase

51
Q

Found in biliary ducts of the liver, in the kidney and pancreas with the largest amounts being in kidney

A

a-glutamyltrasferase (ggt,agt)

52
Q

Found in high concentrations in pancreas and salivary glands where it is secreted to digest complex carbohydrates

A

amylase

53
Q

are unbranched polymers composed of repeating patterns called nucleotides

A

nucleic acids

54
Q
  • stores genetic information of an organism
  • has million nucleotides
  • is contained in the chromosomes of nucleus, each chromosome having a different type
A

DNA

55
Q
  • translates this genetic information into synthesis of proteins
  • has thousand nucleotides
A

RNA

56
Q

human chromosomes

A

46 (23 pairs)

57
Q

is a portion of the DNA molecule responsible for the synthesis of a single protein

A

gene

58
Q
  • A monosaccharide + a base + phosphate
  • is formed by joining the anomeric carbon of the monosaccharide with a nitrogen- atom of the base.
A

nucleotide

59
Q

3 parts of nucleotide

A

a) Nitrogen-containing base
b) Sugar (monosaccharide)
c) Phosphate group

60
Q

nitrogen atom at the 1 position bonds with the 1’ carbon of sugar

A

pyrimidine bases

61
Q

nitrogen atom at the 9 position bonds with the 1’ carbon of the sugar

A

purine bases

62
Q

• DNA
Abbreviation: A
Nucleotide: Deoxyadenosine 5’-monophosphate Abbreviation: dAMP
• RNA
Nucleotide: Adenosine 5’-monophosphate Abbreviation: AMP

A

adenine

63
Q

• DNA
Abbreviation: G
Nucleotide: Deoxyguanosine 5’- monophosphate
Abbreviation: dGMP
• RNA
Nucleotide: Guanosine 5’-monophosphate Abbreviation: GMP

A

guanine

64
Q

• DNA
Abbreviation: C
Nucleotide: Deoxycytidine 5’-monophosphate Abbreviation: dCMP
• RNA
Nucleotide: Cytidine 5’-monophosphate Abbreviation: CMP

A

cytosine

65
Q

• DNA
Abbreviation: T
Nucleotide: Deoxythymidine 5’-monophosphate Abbreviation: dTMP

A

thymine

66
Q

• RNA
Abbreviation: U
Nucleotide: Uridine 5’-monophosphate Abbreviation: UMP

A

uracil

67
Q
  • The combination of sugar + Base
  • monosaccharide + base
A

nucleoside

68
Q

difference of DNA and RNA

A

o DNA contains the sugar deoxyribose, while RNA contains the sugar ribose.
o DNA is a double-stranded molecule while RNA is a single stranded molecule.
• DNA is stable under alkaline conditions while RNA is not stable.

69
Q

first to describe the three- dimensional structure of DNA in 1953

A

James Watson and Francis Crick

70
Q

describes the manner in which the nitrogenous bases of the DNA molecules align with each other

A

Complementary base pairing

71
Q

The DNA molecule is composed of two strands held together by hydrogen bonds. A single strand is different at its two ends. One end is called 5’ (5 prime), the other is called 3’ (3 prime).

A

antiparallel strands

72
Q

are piece of DNA that carry the genetic instructions, or genes of an eukaryote or prokaryote organism

A

chromosomes

73
Q

are organism with a simple cellular structure in which there is no sure nucleus surrounded by a nuclear membrane and there are no true membrane bound organelles

A

prokaryotes

74
Q

are organism that have cells containing a true nucleus enclosed by a nuclear membrane

A

eukaryotes

75
Q
  • The flow of information from DNA to RNA to protein is termed as the _____ of molecular biology. (except with viruses)
A

“central dogma”

76
Q

is the process by which DNA makes a copy of itself when a cell divides

A

replication

77
Q

is the ordered synthesis of RNA from DNA. In this process, the genetic information stored in DNA is passed into RNA.

A

transcription

78
Q

is the synthesis of proteins from RNA. In this process, the genetic message contained in RNA determines the specific amino acid sequence of a protein.

A

translation

79
Q

unwinds and separates double stranded DNA as it moves along the DNA

A

DNA helicase

80
Q

a type of RNA polymerase that generates RNA primers

A

DNA primase

81
Q

synthesize new DNA molecules by adding nucleotides to leading and lagging DNA strands

A

DNA polymerases

82
Q

unwinds and rewinds DNA strands to prevent the DNA from becoming tangled or supercoiled

A

Topoisomerase or DNA Gyrase

83
Q

group of enzymes that remove nucleotide bases from the end of a DNA chain

A

exonucleases

84
Q

joins DNA fragments together by forming phosphodiester bonds between nucleotides

A

DNA ligase

85
Q

From Latin word transcribe and simply means “to make a copy”. Thus, in this process, part of the information in the DNA is copied into a strand of RNA.

A

RNA transcription

86
Q
  • carries the genetic information for protein from DNA to the ribosomes. It is a complimentary RNA copy of a gene on the DNA
  • 750 nucleotides
A

Messenger RNA (mRNA)

87
Q

Is a structural and functional component of the ribosomes, which are “platforms” on which protein synthesis occurs

A

Ribosomal RNA (rRNA)

88
Q
  • translate the genetic code of the mRNA into the primary sequence of amino acids in the protein.
  • Contain 73-93 nucleotides per chain.
A

Transfer RNA (tRNA)

89
Q

are enzymes that transcribe DNA into RNA. Using a DNA template, RNA polymerase builds a new RNA molecule through base pairing.

A

RNA polymerase

90
Q

• It involves translating the genetic information from the sequence of nucleotides into the sequence of amino acids in the primary structure of protein.
• Protein

A

RNA translation

91
Q

is the change in sequence of nucleotide of DNA

A

mutation

92
Q

It occurs as a result of replacement of one nucleotide by other in specific nucleotide sequence of gene

A

point mutation

93
Q

• It is also known as neutral mutation.
• It is the mutation in which mutated codon codes same amino acids as the original codon.

A

silent mutation

94
Q

In this mutation mutated codon codes different amino acid (other than original)

A

missense mutation

95
Q

Mutation in which altered codon is stop codon or chain terminating codon, such mutation is called non-sense mutation

A

nonsense mutation

96
Q

It occurs as a result of addition or deletion of nucleotide in the sequence of DNA

A

frameshift mutation

97
Q

any chemical that cause a change in the DNA sequence

A

mutagens

98
Q

is caused by mutations in genes that are involved in repairing damaged DNA

A

xeoderma pigmentosum

99
Q

is a piece of DNA having its own replication origin so that it can be replicated inside a host cell.

A

DNA cloning vector

100
Q

using recombinant DNA technology to modify an organism’s DNA to achieve desirable traits.

A

genetic engineering

biochem lec (1 decks)

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