enzymes p2 nucleotides 1,2 finals Flashcards

(100 cards)

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
is a substance that slows or stops the normal catalytic function of an enzyme by binding to it
enzyme inhibitor
26
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
competitive enzyme inhibitor
27
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.
reversible competitive inhibition
28
is a molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site
noncompetitive enzyme inhibitor
29
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
reversible noncompetitive inhibition
30
Occurs when (II) binds only to the enzyme- substrate complex (ESES) and not free EE.
uncompetitive inhibition
31
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
irreversible enzyme inhibitor
32
inhibitors do not have structures similar to that of enzyme’s normal substrate
irreversible inhibition
33
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.
regulation of the enzyme activity
34
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.
allosteric enzymes
35
inhibit enzyme action
negative allosterism
36
stimulate enzyme action
positive allosterism
37
The production of the enzyme in an active form.
proenzyme
38
This is a process in which a chemical group is covalently added to or removed from the protein.
protein modification
39
It is an enzyme regulation process in which formation of a product inhibits an earlier reaction in the sequence.
feedback control
40
refers to the enzymes that are used directly or as components of the assay system for the determination of number of substances
diagnostic enzymes
41
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.
serum
42
➜ 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)
lactate dehydrogenase
43
is found predominantly in heart muscle, kidney and in RBCs
LDH1 and LDH2
44
is found in a variety of tissues such as spleen, lung, endocrine glands and lymph nodes
LDH3
45
found in liver, skin and skeletal muscle is the least stable and runs the shortest on electrophoresis
LDH4 and LDH5
46
o Formally known as glutamate pyruvate transaminase (GPT) o Found in high concentrations in liver cells and in much smaller concentrations elsewhere.
alanine transaminase
47
➜ 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.
alkaline phosphatase
48
➜ Also known as creatine phosphatase (CPK) ➜ Mainly found in heart and skeletal muscle and in brain
creatine kinase
49
➜ 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
acid phosphatase
50
➜ The enzyme catalyze the hydrolysis of choline esters ➜ Presence is assumed when the muscle relaxant scoline is administered.
cholinesterase
51
Found in biliary ducts of the liver, in the kidney and pancreas with the largest amounts being in kidney
a-glutamyltrasferase (ggt,agt)
52
Found in high concentrations in pancreas and salivary glands where it is secreted to digest complex carbohydrates
amylase
53
are unbranched polymers composed of repeating patterns called nucleotides
nucleic acids
54
- stores genetic information of an organism - has million nucleotides - is contained in the chromosomes of nucleus, each chromosome having a different type
DNA
55
- translates this genetic information into synthesis of proteins - has thousand nucleotides
RNA
56
human chromosomes
46 (23 pairs)
57
is a portion of the DNA molecule responsible for the synthesis of a single protein
gene
58
- A monosaccharide + a base + phosphate - is formed by joining the anomeric carbon of the monosaccharide with a nitrogen- atom of the base.
nucleotide
59
3 parts of nucleotide
a) Nitrogen-containing base b) Sugar (monosaccharide) c) Phosphate group
60
nitrogen atom at the 1 position bonds with the 1’ carbon of sugar
pyrimidine bases
61
nitrogen atom at the 9 position bonds with the 1’ carbon of the sugar
purine bases
62
• DNA Abbreviation: A Nucleotide: Deoxyadenosine 5’-monophosphate Abbreviation: dAMP • RNA Nucleotide: Adenosine 5’-monophosphate Abbreviation: AMP
adenine
63
• DNA Abbreviation: G Nucleotide: Deoxyguanosine 5’- monophosphate Abbreviation: dGMP • RNA Nucleotide: Guanosine 5’-monophosphate Abbreviation: GMP
guanine
64
• DNA Abbreviation: C Nucleotide: Deoxycytidine 5’-monophosphate Abbreviation: dCMP • RNA Nucleotide: Cytidine 5’-monophosphate Abbreviation: CMP
cytosine
65
• DNA Abbreviation: T Nucleotide: Deoxythymidine 5’-monophosphate Abbreviation: dTMP
thymine
66
• RNA Abbreviation: U Nucleotide: Uridine 5’-monophosphate Abbreviation: UMP
uracil
67
- The combination of sugar + Base - monosaccharide + base
nucleoside
68
difference of DNA and RNA
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
first to describe the three- dimensional structure of DNA in 1953
James Watson and Francis Crick
70
describes the manner in which the nitrogenous bases of the DNA molecules align with each other
Complementary base pairing
71
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).
antiparallel strands
72
are piece of DNA that carry the genetic instructions, or genes of an eukaryote or prokaryote organism
chromosomes
73
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
prokaryotes
74
are organism that have cells containing a true nucleus enclosed by a nuclear membrane
eukaryotes
75
- The flow of information from DNA to RNA to protein is termed as the _____ of molecular biology. (except with viruses)
“central dogma”
76
is the process by which DNA makes a copy of itself when a cell divides
replication
77
is the ordered synthesis of RNA from DNA. In this process, the genetic information stored in DNA is passed into RNA.
transcription
78
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.
translation
79
unwinds and separates double stranded DNA as it moves along the DNA
DNA helicase
80
a type of RNA polymerase that generates RNA primers
DNA primase
81
synthesize new DNA molecules by adding nucleotides to leading and lagging DNA strands
DNA polymerases
82
unwinds and rewinds DNA strands to prevent the DNA from becoming tangled or supercoiled
Topoisomerase or DNA Gyrase
83
group of enzymes that remove nucleotide bases from the end of a DNA chain
exonucleases
84
joins DNA fragments together by forming phosphodiester bonds between nucleotides
DNA ligase
85
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.
RNA transcription
86
- 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
Messenger RNA (mRNA)
87
Is a structural and functional component of the ribosomes, which are “platforms” on which protein synthesis occurs
Ribosomal RNA (rRNA)
88
- translate the genetic code of the mRNA into the primary sequence of amino acids in the protein. - Contain 73-93 nucleotides per chain.
Transfer RNA (tRNA)
89
are enzymes that transcribe DNA into RNA. Using a DNA template, RNA polymerase builds a new RNA molecule through base pairing.
RNA polymerase
90
• It involves translating the genetic information from the sequence of nucleotides into the sequence of amino acids in the primary structure of protein. • Protein
RNA translation
91
is the change in sequence of nucleotide of DNA
mutation
92
It occurs as a result of replacement of one nucleotide by other in specific nucleotide sequence of gene
point mutation
93
• It is also known as neutral mutation. • It is the mutation in which mutated codon codes same amino acids as the original codon.
silent mutation
94
In this mutation mutated codon codes different amino acid (other than original)
missense mutation
95
Mutation in which altered codon is stop codon or chain terminating codon, such mutation is called non-sense mutation
nonsense mutation
96
It occurs as a result of addition or deletion of nucleotide in the sequence of DNA
frameshift mutation
97
any chemical that cause a change in the DNA sequence
mutagens
98
is caused by mutations in genes that are involved in repairing damaged DNA
xeoderma pigmentosum
99
is a piece of DNA having its own replication origin so that it can be replicated inside a host cell.
DNA cloning vector
100
using recombinant DNA technology to modify an organism’s DNA to achieve desirable traits.
genetic engineering