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85 Cards in this Set
- Front
- Back
T/F Enzymes are proteins |
True |
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Proteins that act as a catalyst for biochemical reactions |
Enzymes |
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T/F Enzymes are a true catalyst |
True |
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T/F At the end of the reaction, enzymes converted to something else |
False, enzymes remain unchanged at the end of the reaction |
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What are the secondary structures present in CHYMOTRYPSIN |
Alpha helix, Beta pleated sheet |
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T/F Chymotrypsin is considered as globular protein |
True |
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T/F Enzymes can undergo denaturation |
True |
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T/F Every biochemical reaction in the body is accompanied by an specific enzymes |
True |
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Enzymes are subdivided into two classes; |
Simple Enzyme-only has an amino acid side chain Conjugated Enzyme- has non protein part + protein part |
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Part of the conjugated enzyme that refers to the protein part |
Apoenzyme |
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It includes all the non-protein parts found in the conjugated enzyme |
Cofactor/Coenzyme (one kind of cofactor) |
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Apoenzyme combined with the Cofactor is called ___________. It is the whole conjugated enzyme that is biologically functional/can catalyze reaction |
Holoenzyme |
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Holoenzyme + Substrate = |
Product |
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T/F Substrate is part of the conjugated enzyme |
False |
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Cofactor is subdivided into two: |
•Small Organic Molecules •Inorganic Ion |
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Derives from dietary minerals |
Inorganic Ion |
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Derived from dietary vitamins |
Small Organic Molecules |
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If the co-factor is organic, it has a specific name which is called __________ |
Co-enzyme |
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Minerals for tooth and bone formation |
Calcium |
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Sources of calcium |
Milk and other dietary products |
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For bone development and transfer of energy in cells |
Phosphorus |
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Sources of Phosphorus |
Most foods |
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For nerve transmission and muscle contraction |
Sodium |
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Sources of Sodium |
Meat, salt, dietary products |
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For formation of HCl |
Chlorine |
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Sources of Chlorine |
Salt |
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For regulation of hearbeat, maintainance of water balance, nerve transmission |
Potassium |
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Sources of Potassium |
Fruit(banana) |
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For catalyst for ATP formation |
Magnesium |
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Sources of Magnesium |
Nuts, grains, dark green vegetables, sea food, chocolate |
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For thyroid activity |
Iodine |
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Sources of iodine |
Sea foods, salt |
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For Hemoglobin formation |
Iron |
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Sources of Iron |
Meat, green vegetables, dried fruits |
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Reactant in an enzyme-catalyzed reaction |
Substrate |
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The suffix -in found in the name of some __________ enzymes |
Digestive |
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Enzymes that catalyzes an oxidation reaction |
Oxidase |
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Enzymes that catalyze a hydrolysis reaction |
Hydrolase |
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Enzymes can be named based on what? |
•Type of Reaction •Identity of the substrate •General nature of Substrate |
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Who created/developed the name of the enzymes and anything else that is related to biochemistry |
International Union of Biochemistry and Molecular Biology (IUBMB) |
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Major class of enzyme that involves oxidation-reduction reaction catalyzed |
Oxidoreductases |
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Major class of enzyme that involves the reaction of functional group transfer reactions |
Transferases |
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Major class that involves hydrolysis reaction |
Hydrolases |
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Major Class that involves the reactions involving addition or removal of groups form double bonds |
Lyases |
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Major class that involves isomeration reactions |
Isomerase |
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Major class that reactions involving bond formation coupled with ATP hydrolysis |
Ligases |
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Enzymes under oxidoreductase that involves oxidation of the substrate |
Oxidase |
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Enzymes under oxidoreductase that involves reduction of the substrate |
Reductases |
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Enzymes under oxidoreductase that involves the introduction of a double bond (oxidation) by formal removal of 2 H atoms from substrate, the H being accepted by a coenzyme |
Dehydrogenases |
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Enzymes under transferases that involves the transfer of an amino group between substrates |
Transaminases |
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Enzymes under transferases that involves the transfer of a phosphate group between substrates |
Kinases |
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Enzymes under hydrolase that involves the hydrolysis of ester linkages in lipids |
Lipases |
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Enzymes under hydrolase that involves the hydrolysis of amide linkages in protein |
Proteases |
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Enzymes under hydrolase that involves the hydrolysis of sugar-phosphate ester bonds in nucleic acid |
Nucleases |
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Enzymes under hydrolase that involves the hydrolysis of glycosidic bonds in carbohydrates |
Carbohydrases |
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Enzymes under hydrolase that involves the hydrolysis of phosphate-ester bonds |
Phosphotases |
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Enzymes under lyases that involves the removal of H2O from substrate |
Dehydratases |
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Enzymes under lyases that involves the removal of CO2 from substrate |
Decarboxylases |
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Enzymes under lyases that involves the removal of NH3 from substrate |
Deaminases |
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Enzymes under lyases that involves the addition of H2O to a substrate |
Hydratases |
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Enzymes under isomerases that involves the conversion of D to L isomer or vice versa |
Racemases |
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Enzymes under isomerases that involves the transfer of a functional group from one position to another in the same molecule (has only one reactant and one product) |
Mutases |
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Enzymes under ligases that involves the formation of new bond between 2 substrates with participation of ATP |
Synthetases |
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Enzymes under ligases that involves the formation of new bond between a substrate and CO2 with participation of ATP |
Carboxylases |
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Specific location found in the enzyme where the substrate binds |
Active site |
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T/F Enzymes only have 1 active site |
False |
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Intermediate reaction species formed when substrate binds with the active site |
Enzyme Substrate Complex |
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T/F There are 3 models for substrate binding to enzymes |
False, 2 only •Lock and key model •Induced Fit model |
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Who proposed the lock and key model |
Fischer |
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Who proposed the Induced Fit model |
Koshland |
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T/F Fischer mechanism has an active site that fixed in shape |
True |
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T/F Koshland Mechanism has an active site that adapts to substrate |
True |
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T/F Active site is symmetric |
False |
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T/F There is no reaction between the substrate and the sidechains of amino acids in the enzymes |
False |
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Each enzyme molecule can transform __________ substrate molecules into product each second |
100-1000 |
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T/F Enzymes are 10^3-10^8 faster than uncatalyzed reaction |
True |
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Catalytic Efficiency |
Gano ka efficient enzymes |
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The number of substrate molecules that an enzyme molecule can process per second when saturated with the substrate |
Turnover number |
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T/F Turnover number is equivalent to the catalytic rate constant (kcat) |
True |
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T/F Enzymes are lowly specific |
False |
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T/F Enzymes can interact with more substrate |
False, 1 or few only |
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T/F Enzymes can catalyze 2 types of chemical reaction |
False, only 1 |
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Nonprotein portion of the enzyme that is needed for enzymic activity |
Cofactor |
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T/F Enzymes can be activated or inhibited so that the rate of product formation responds to the need of the cell |
True |
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T/F Many enzymes are localized in specific organelles within the cell (compartmentalized) |
True |