Enzymes PPT based Flashcards
(102 cards)
1
Q
is a compound or biological polymer, usually a protein, that acts as a catalyst for a biochemical reaction.
A
ENZYMES
2
Q
Biological catalyst for chemical reaction in biological system
A
Enzymes
3
Q
is an enzyme composed only of protein (amino acids) not bound to any nonproteins
A
simple enzyme
4
Q
is an enzyme that has a nonprotein part in addition to a protein part
A
conjugated enzyme
5
Q
is the protein part of a conjugated enzyme or holoenzyme
A
apoenzyme
6
Q
enzyme lacking an essential cofactor
A
apoenzyme
7
Q
serve functions similar to those of prosthetic groups but bind in a transient, dissociable manner either to the enzyme or to a substrate such as ATP
A
cofactor
8
Q
Tightly bound cofactor to the apoenzyme
A
prosthetic group
9
Q
is the biochemically active conjugated enzyme produced from an apoenzyme and a cofactor
A
holoenzyme
10
Q
Intact and functional enzyme containing all cofactors/ coenzyme
A
holoenzyme
11
Q
is a small organic molecule that serves as a cofactor in a conjugated enzyme
A
Coenzyme or cosubstrate
12
Q
the inorganic cofactor
A
Coenzyme or cosubstrate
13
Q
is the reactant in an enzyme-catalyzed reaction
A
Substrate (S)
14
Q
biomolecule that enzymes react with
A
Substrate (S)
15
Q
the biomolecules formed by enzyme mediated reactions
A
Product (P)
16
Q
Enzymes that require a metal ion cofactor
A
metal-activated enzymes
17
Q
enzymes that contain tightly bound metal ions
A
metalloenzymes
18
Q
are distinguished by their tight, stable incorporation into a protein’s structure by covalent or noncovalent forces.
A
Prosthetic groups
19
Q
______ are the most common prosthetic groups
A
Metals
20
Q
The roughly one-third of all enzymes that contain tightly bound metal ions are termed ______
A
metalloenzymes
21
Q
serve functions similar to those of prosthetic groups but bind in a transient, dissociable manner either to the enzyme or to a substrate such as ATP.
A
Cofactors
22
Q
Unlike the stably associated prosthetic groups, _____ therefore must be present in the medium surrounding the enzyme for catalysis to occur.
A
cofactors
23
Q
Metalloenzyme:
Destroy superoxide anion
A
Superoxide dismutase
24
Q
Metalloenzyme:
They oxidize a range of aliphatic and aromatic alcohols to their corresponding aldehydes and ketones using NAD+ as a coenzyme
A
Alcohol dehydrogenase
25
Metalloenzyme:
Synthesize DNA
DNA polymerase
26
Metalloenzyme:
is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy terminal (C-terminal) end of a protein or peptide
Carboxypeptidase A
27
Metalloenzyme:
Synthesize oxaloacetate
Pyruvate carboxylase
28
Metalloenzyme:
Synthesize Urea
Arginase
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Metalloenzyme:
transports oxygen from the lungs to the capillaries of the tissue
Hemoglobins
30
Metalloenzyme:
carry electrons between two segments of the electron-transport chain.
Cytochromes
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Metalloenzyme:
hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains
Cytochrome Oxidase
32
the suffix “______” is added to the name of the substrate
“ase”
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CLASSIFICATION OF ENZYME:
acts on starch
amylase
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CLASSIFICATION OF ENZYME:
acts on maltose
maltase
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CLASSIFICATION OF ENZYME:
act on urea
cellulase
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CLASSIFICATION OF ENZYME:
acts on fats
lipase
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CLASSIFICATION OF ENZYME (except for):
in gastric juice (stomach
Pepsin
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CLASSIFICATION OF ENZYME (except for):
in pancreatic juice (small intestine)
Trypsin
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CLASSIFICATION OF ENZYME (except for):
in saliva
Ptyalin
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CLASSIFICATION OF ENZYME (except for):
the milk curding enzyme
Rennin
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NOMENCLATURE and CLASSIFICATION OF ENZYME:
oxidation reaction
Oxidase
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NOMENCLATURE and CLASSIFICATION OF ENZYME:
decarboxylation
decarboxylase
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NOMENCLATURE and CLASSIFICATION OF ENZYME:
transamination
transaminase
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NOMENCLATURE and CLASSIFICATION OF ENZYME:
hydrolysis
hydrolase
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NOMENCLATURE and CLASSIFICATION OF ENZYME:
reversible addition or removal of water
hydrase or dehydrase
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is an enzyme that catalyzes an oxidation–reduction reaction.
OXIDOREDUCTASE
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an oxidation that increases the number of C-O bonds and/or decreases the number of C-H bonds
ORGANIC OXIDATION rxn
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a reduction that decreases the number of C-O bonds and/or increases the number of C-H bonds
ORGANIC REDUCTION rxn
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“browning reaction” caused by _______ (or polyphenoloxidase), a conjugated enzyme in which copper is present:
phenolase
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is an enzyme that catalyzes the transfer of a functional group other than hydrogen (ex. methyl, acyl, amino or phosphate groups) from one molecule to another
TRANSFERASES
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Example of Oxidoreductase
Lactate dehydrogenase
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Example of Transferases
transaminases and kinases
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is an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break
HYDROLASE
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Hydrolysis reactions are central to the process of _______
digestion
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Example of Hyrdolase:
breaking of glycosidic bonds in oligo- and polysaccharides
Carbohydrases
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Example of Hyrdolase:
breaking of peptide linkages in proteins
Proteases
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Example of Hyrdolase:
breaking of ester linkages in triacylglycerols.
lipases
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is an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation.
LYASE
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Example of Lyase:
effects the removal of the components of water from a double bond
Dehydratase
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Example of Lyase:
effects the addition of the components of water to a double bond
Hydratase
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an enzyme that catalyzes the isomerization (rearrangement of atoms or interconversion of optical, geometric, or positional isomers of a substrate in a reaction, converting it into a molecule isomeric with itself. There is only one reactant and one product in reactions where isomerases are operative
ISOMERASE
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an enzyme that catalyzes the bonding together of two molecules into one with the participation of ATP
LIGASE or SYNTHETASE
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Main Classes and Subclasses of Enzymes:
oxidation of a substrate
OXIDOREDUCTASES, oxidases
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Main Classes and Subclasses of Enzymes:
reduction of a substrate
OXIDOREDUCTASES, reductases
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Main Classes and Subclasses of Enzymes:
introduction of double bond (oxidation) by formal removal of two H atoms from substrate, the H being accepted by a coenzyme
OXIDOREDUCTASES, dehydrogenases
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Main Classes and Subclasses of Enzymes:
transfer of an amino group between substrates
TRANSFERASES, Transaminases
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Main Classes and Subclasses of Enzymes:
transfer of a phosphate group between substrates
TRANSFERASES, Kinases
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Main Classes and Subclasses of Enzymes:
hydrolysis of ester linkages in lipids
HYDROLASES, Lipases
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Main Classes and Subclasses of Enzymes:
hydrolysis of amide linkages in proteins
HYDROLASES, Proteases
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Main Classes and Subclasses of Enzymes:
hydrolysis of sugar–phosphate ester bonds in nucleic acid
HYDROLASES, Nucleases
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Main Classes and Subclasses of Enzymes:
hydrolysis of glycosidic bonds in carbohydrates
HYDROLASES, Carbohydrases
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Main Classes and Subclasses of Enzymes:
hydrolysis of phosphate–ester bonds
HYDROLASES, phosphatases
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Main Classes and Subclasses of Enzymes:
removal of H2O from a substrate
LYASES, dehydratases
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Main Classes and Subclasses of Enzymes:
removal of CO2 from a substrate
LYASES, decarboxylases
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Main Classes and Subclasses of Enzymes:
removal of NH3 from a substrate
LYASES, deaminases
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Main Classes and Subclasses of Enzymes:
addition of H2O to a substrate
LYASES, hydratases
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Main Classes and Subclasses of Enzymes:
conversion of D isomer to L isomer,or vice versa
ISOMERASES, Racemases
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Main Classes and Subclasses of Enzymes:
transfer of a functional group from one position to another in the same molecule
ISOMERASES, Mutases
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Main Classes and Subclasses of Enzymes:
formation of new bond between two substrates, with participation of ATP
LIGASES, Synthetases
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Main Classes and Subclasses of Enzymes:
formation of new bond between a substrate and CO2, with participation of ATP
LIGASES, Carboxylases
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the relatively small part of an enzyme’s structure that is involved in catalysis. Usually a “crevicelike” location the enzyme.
Enzyme Active Site
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the intermediate reaction species that is formed when the substrate bind to the active site of an enzyme.
Enzyme-Substrate Complex
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only a substrate whose shape and chemical nature are complementary to those of the active site can interact with the enzyme.
Lock-and-Key Model
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- is a result of the enzyme’s flexibility
- the enzyme active site, although not exactly complementary in shape to that of the substrate, is flexible enough that it can adapt to the shape of the substrate.
Induced-Fit Model
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the extent to which an enzyme’s activity is restricted to a specific substrate, a specific group of substrates, a specific type of chemical bond, or a specific type of chemical reaction
Enzyme specificity
86
FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:
Reaction rate increases with _____ until the point at which the protein is denatured and activity drops sharply.
Temperature
87
FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:
Maximum enzymatic activity is possible only within a narrow ____ range; outside this ___ range, the protein is denatured and activity drops sharply.
pH
88
FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:
Reaction rate increases with _______ until full saturation occurs; then the rate levels off.
Concentration of Substrate/Substrate Concentration
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FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:
Reaction rate increases with increasing ______, assuming enzyme concentration is much lower than that of substrate.
Concentration of Enzyme/Enzyme Concentration
90
is a microorganism that thrives in extreme environments, environments in which humans and most other forms of life could not survive.
Extremophile
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is a microbial enzyme active at conditions that would inactivate human enzymes as well as enzymes present in other types of higher organisms.
EXTREMOZYME
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Uses of this include:
- detergent formulations
- the petroleum industry during oil well drilling operations
EXTREMOZYME
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Extremophile:
optimal growth at pH levels of 3.0 or below
acidophiles
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Extremophile:
optimal growth at pH levels of 9.0 or above
alkaliphiles
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Extremophile:
a salinity that exceeds 0.2 M NaCl needed for growth
halophiles
96
Extremophile:
a temperature between 80°C and 122°C needed to thrive
Hypothermophiles
97
Extremophile:
a temperature of 15°C or lower needed for growth
cryophiles
98
Extremophile:
a high hydrostatic pressure needed for growth
piezophiles
99
commonly called H. pylori, is a bacterium that can function in them highly acidic environment of the stomach
* causes more than 90% of duodenal ulcers and up to 80% of gastric ulcers.
Helicobacter pylori
100
a molecule closely resembling the substrate. Binds to the active site and temporarily prevents substrates form occupying
Competitive Enzyme Inhibitor
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a molecule that binds to a site on an enzyme that is not the active site. The normal substrate still occupies the active site
Noncompetitive Enzyme Inhibitor
102
a molecule that forms a covalent bond to a part of the active site, permanently preventing substrate from occupying.
Irreversible Enzyme Inhibitor
