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85 Cards in this Set

  • Front
  • Back

T/F Enzymes are proteins

True

Proteins that act as a catalyst for biochemical reactions

Enzymes

T/F Enzymes are a true catalyst

True

T/F At the end of the reaction, enzymes converted to something else

False, enzymes remain unchanged at the end of the reaction

What are the secondary structures present in CHYMOTRYPSIN

Alpha helix, Beta pleated sheet

T/F Chymotrypsin is considered as globular protein

True

T/F Enzymes can undergo denaturation

True

T/F Every biochemical reaction in the body is accompanied by an specific enzymes

True

Enzymes are subdivided into two classes;

Simple Enzyme-only has an amino acid side chain


Conjugated Enzyme- has non protein part + protein part

Part of the conjugated enzyme that refers to the protein part

Apoenzyme

It includes all the non-protein parts found in the conjugated enzyme

Cofactor/Coenzyme (one kind of cofactor)

Apoenzyme combined with the Cofactor is called ___________. It is the whole conjugated enzyme that is biologically functional/can catalyze reaction

Holoenzyme

Holoenzyme + Substrate =

Product

T/F Substrate is part of the conjugated enzyme

False

Cofactor is subdivided into two:

•Small Organic Molecules


•Inorganic Ion

Derives from dietary minerals

Inorganic Ion

Derived from dietary vitamins

Small Organic Molecules

If the co-factor is organic, it has a specific name which is called __________

Co-enzyme

Minerals for tooth and bone formation

Calcium

Sources of calcium

Milk and other dietary products

For bone development and transfer of energy in cells

Phosphorus

Sources of Phosphorus

Most foods

For nerve transmission and muscle contraction

Sodium

Sources of Sodium

Meat, salt, dietary products

For formation of HCl

Chlorine

Sources of Chlorine

Salt

For regulation of hearbeat, maintainance of water balance, nerve transmission

Potassium

Sources of Potassium

Fruit(banana)

For catalyst for ATP formation

Magnesium

Sources of Magnesium

Nuts, grains, dark green vegetables, sea food, chocolate

For thyroid activity

Iodine

Sources of iodine

Sea foods, salt

For Hemoglobin formation

Iron

Sources of Iron

Meat, green vegetables, dried fruits

Reactant in an enzyme-catalyzed reaction

Substrate

The suffix -in found in the name of some __________ enzymes

Digestive

Enzymes that catalyzes an oxidation reaction

Oxidase

Enzymes that catalyze a hydrolysis reaction

Hydrolase

Enzymes can be named based on what?

Type of Reaction


•Identity of the substrate


•General nature of Substrate

Who created/developed the name of the enzymes and anything else that is related to biochemistry

International Union of Biochemistry and Molecular Biology (IUBMB)

Major class of enzyme that involves oxidation-reduction reaction catalyzed

Oxidoreductases

Major class of enzyme that involves the reaction of functional group transfer reactions

Transferases

Major class that involves hydrolysis reaction

Hydrolases

Major Class that involves the reactions involving addition or removal of groups form double bonds

Lyases

Major class that involves isomeration reactions

Isomerase

Major class that reactions involving bond formation coupled with ATP hydrolysis

Ligases

Enzymes under oxidoreductase that involves oxidation of the substrate

Oxidase

Enzymes under oxidoreductase that involves reduction of the substrate

Reductases

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

Enzymes under transferases that involves the transfer of an amino group between substrates

Transaminases

Enzymes under transferases that involves the transfer of a phosphate group between substrates

Kinases

Enzymes under hydrolase that involves the hydrolysis of ester linkages in lipids

Lipases

Enzymes under hydrolase that involves the hydrolysis of amide linkages in protein

Proteases

Enzymes under hydrolase that involves the hydrolysis of sugar-phosphate ester bonds in nucleic acid

Nucleases

Enzymes under hydrolase that involves the hydrolysis of glycosidic bonds in carbohydrates

Carbohydrases

Enzymes under hydrolase that involves the hydrolysis of phosphate-ester bonds

Phosphotases

Enzymes under lyases that involves the removal of H2O from substrate

Dehydratases

Enzymes under lyases that involves the removal of CO2 from substrate

Decarboxylases

Enzymes under lyases that involves the removal of NH3 from substrate

Deaminases

Enzymes under lyases that involves the addition of H2O to a substrate

Hydratases

Enzymes under isomerases that involves the conversion of D to L isomer or vice versa

Racemases

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

Enzymes under ligases that involves the formation of new bond between 2 substrates with participation of ATP

Synthetases

Enzymes under ligases that involves the formation of new bond between a substrate and CO2 with participation of ATP

Carboxylases

Specific location found in the enzyme where the substrate binds

Active site

T/F Enzymes only have 1 active site

False

Intermediate reaction species formed when substrate binds with the active site

Enzyme Substrate Complex

T/F There are 3 models for substrate binding to enzymes

False, 2 only


•Lock and key model


•Induced Fit model

Who proposed the lock and key model

Fischer

Who proposed the Induced Fit model

Koshland

T/F Fischer mechanism has an active site that fixed in shape

True

T/F Koshland Mechanism has an active site that adapts to substrate

True

T/F Active site is symmetric

False

T/F There is no reaction between the substrate and the sidechains of amino acids in the enzymes

False

Each enzyme molecule can transform __________ substrate molecules into product each second

100-1000

T/F Enzymes are 10^3-10^8 faster than uncatalyzed reaction

True

Catalytic Efficiency

Gano ka efficient enzymes

The number of substrate molecules that an enzyme molecule can process per second when saturated with the substrate

Turnover number

T/F Turnover number is equivalent to the catalytic rate constant (kcat)

True

T/F Enzymes are lowly specific

False

T/F Enzymes can interact with more substrate

False, 1 or few only

T/F Enzymes can catalyze 2 types of chemical reaction

False, only 1

Nonprotein portion of the enzyme that is needed for enzymic activity

Cofactor

T/F Enzymes can be activated or inhibited so that the rate of product formation responds to the need of the cell

True

T/F Many enzymes are localized in specific organelles within the cell (compartmentalized)

True