Enzyme Types Review PDF

ENZYMES-TYPES OF ENZYMES REVIEWER They are selective and control the chemical reaction in the cell: ENZYMES Macromolecules that compose enzymes: PROTEINS The molecule binding to the enzyme is called: SUBSTRATE What is formed when the enzyme and substrate meet? ENZYME-SUBSTRATE COMPL...

ENZYMES-TYPES OF ENZYMES REVIEWER They are selective and control the chemical reaction in the cell: ENZYMES Macromolecules that compose enzymes: PROTEINS The molecule binding to the enzyme is called: SUBSTRATE What is formed when the enzyme and substrate meet? ENZYME-SUBSTRATE COMPLEX What is formed when the enzyme and substrate undergo chemical reaction? PRODUCTS The shape of enzymes: GLOBULAR The bonds that exist between enzymes: INTRAMOLECULAR & INTERMOLECULAR BONDS The most important factor or characteristic for an efficient binding of enzyme and substrate is the enzyme’s: SHAPE The strong bonds existing between single atoms: INTRAMOLECULAR BONDS The weak bonds existing between separate molecules: INTERMOLECULAR BONDS Covalent and ionic bonds contain which type of bonds? INTRAMOLECULAR BONDS Hydrogen bonding in water contains which type of bonds? INTERMOLECULAR BONDS Non-protein chemical compounds that help catalyze biological reactions: COFACTORS Helper molecules are also called: COFACTORS The organic cofactors are: PROSTHETIC GROUP & COENZYMES Metallic ions are considered: INORGANIC Without the cofactor attached, the protein or enzyme is said to be: INACTIVE This is not an enzyme but works with enzymes to help in the catalytic activity: COENZYME It is bound loosely to the enzyme: COENZYMES They have the ability to recognize, attract, or repulse a substrate or product: COENZYME Coenzymes are derived from: VITAMINS Among the organic cofactors, which is not naturally synthesized in the body? COENZYMES These can carry or shuttle chemical groups from one enzyme to another enzyme: COENZYMES Inactive enzyme with any metal ions or cofactor attached to it, that is ready to catalyze a reaction: HOLOENZYME A complete functional enzyme: HOLOENZYME These temporarily bind to the active site, giving an intense positive charge to the enzyme’s proteins: ACTIVATORS Also known as the inactive enzyme where in, the cofactor is removed: APOENZYME For apoenzymes to function, it needs to have a _______ attached to it: COFACTOR Holoenzyme contains a protein factor called: INACTIVE ENZYME or APOENZYME Holoenzyme contains a non-protein factor called: COFACTOR Holoenzyme is the: COMPLETE ENZYME Prosthetic groups are attached to proteins via: COVALENT BOND These are firmly/tightly bounded and cannot be removed easily: PROSTHETIC GROUPS How many different digestive enzymes are produced in the body? 22 These are biological catalysts that speed up a chemical reaction: ENZYMES This is the energy needed to start any chemical reaction: ACTIVATION ENERGY When the enzymatic concentration is high, what is lowered? ACTIVATION ENERGY The location where the enzyme and substrate binds: ACTIVE SITE These combine temporarily with es or enzyme-substrate complex: COENZYMES This is the nature of enzymes in which they are highly selective because its shape must fit with the substrate: NATURE OF SPECIFICITY How many models are there presenting the interaction of an enzyme to a substrate? TWO Give the two models: LOCK & KEY MODEL and INDUCED FIT MODEL The lock and key model was proposed by: EMIL FISCHER , In the year: 1894 The induced fit model was proposed by: DANIEL KOSHLAND, In the year: 1958 Chemicals that interfere with enzyme function and disrupt the successful binding of enzyme and substrate: INHIBITORS A molecule that mimics the substrate, blocking the active site, and competing with the substrate: COMPETITVE INHIBITOR Does not compete for the active site but attaches to a different place in the enzyme to change its shape. NON-COMPETITIVE INHIBITOR The location or site where the non-competitive inhibitor attaches: ALLOSTERIC SITE This is the loss or gain of electrons: REDOX REACTIONS Redox means __________ : REDUCTION-OXIDATION  Glucose is an example of a ______ molecule: REDUCED NAD + is an example of an _________ molecule: OXIDIZED NADH is an example of a ________ molecule: REDUCED When a molecule is oxidized, it ______ electrons: LOST When a molecule is reduced, it _____ electrons: GAINED What is released during a cell’s oxidation of glucose? ENERGY Identify whether Lock and key model or Induced fit model: 1.Which model has the perfect binding of specific substrate and enzyme in the active site? LOCK AND KEY 2.There is no shape change by the substrate to the active site. LOCK AND KEY 3.The enzyme is very rigid and not flexible. LOCK AND KEY 4.The shape of the active site is complementary to the substrate: LOCK AND KEY 5.There is just a single substrate binding: LOCK AND KEY 6.The substrate binding to the enzyme is very fit: LOCK AND KEY 7. It can’t stabilize the transition state from es complex to products. LOCK AND KEY 8. These are amino acids present in the active site repositioning, orienting, and breaking the bonds in the substrate to make it fit the enzyme: CATALYTIC GROUPS OR CATALYTIC RESIDUES 9. This model induced conformational changes in the active site: INDUCED FIT 10. The enzyme has a flexible structure: INDUCED FIT 11. The shape is non-complementary to substrate: INDUCED FIT 12. Variety of substrates can bind with the active site due to conformational changes: INDUCED FIT 13. It can explain the transition state from es complex to products: INDUCED FIT 14. This model supports the presence of competitive and non-competitive inhibitors and noise in the background: INDUCED FIT True or false: Enzymes are consumed during the reaction and changed at the end of every reaction. FALSE (enzymes remain the same all throughout the reaction, it’s not used up) Enzymes can speed up the rate of reaction without changing the position of the equilibrium. TRUE Enzymes can participate in other chemical reactions because it is specific. FALSE (it is specific so, it will only participate in specific chemical reactions, not in every reaction) Substrate is the location where reactions are catalyzed to make products. FALSE (active site is where the reactions happen) The length of enzymes is the most crucial element or factor for an efficient enzyme-substrate binding. FALSE (shape is the most crucial element or factor) The substrate continuously changes until the active site completely binds with the enzyme. FALSE (active site is what’s being continuously changed until the substrate binds with the enzyme) TYPES OF ENZYMES – “LILHOT” (LYASE, ISOMERASE, LIGASE, HYDROLASE, OXYDOREDUCTASE, TRANSFERASE) Catalyzes redox reactions: OXYDOREDUCTASE Examples: cytochrome oxidase and lactate dehydrogenase An enzyme that involves the transfer of electrons from one molecule to another: OXYDOREDUCTASE  An enzyme that catalyzes transfer of functional groups or groups of atoms from one molecule to another. TRANSFERASE Example: Acetate kinase Involves the cleavage or splitting of substrates and chemical bonds by water /hydrolysis. HYDROLASE Example: lipase and sucrose This enzyme splits chemical bonds without using water. It also forms double bonds vis removal of groups. LYASE Example: Isocitrate lyase This enzyme rearranges atoms or transfers groups of atoms from one position to another within the molecule. ISOMERASE Example: glucose-phosphate isomerase This enzyme joins two molecules or atoms to form a chemical bond. LIGASE Example: DNA LIGASE, Acetyl CoA synthetase COENZYME EXAMPLES: VITAMIN B12, VITAMIN C , NAD+, NADP+, FMN PROSTHETIC GROUP EXAMPLES: HEME GROUP, FLAVIN GROUP, BIOTIN, PLP, TPP HAPPY REVIEWING, EVERYONE! BEST OF LUCK! - Ma’Am Rheanne