front 1 What is metabolism? | back 1 totality of the physical and chemical processes that occur in a cell |
front 2 What is anabolism? | back 2 synthesis of cell PRODUCTS; REQUIRES ENERGY building up (ex. building up of glucose to make glycogen) |
front 3 What is catabolism? | back 3 Breakdown of LARGER molecules into SMALLER ones; RELEASES energy; pathways of metabolic schemes are generally complex and detailed |
front 4 ALL biochemical reactions need | back 4 the presence of a specific and special class of proteins called ENZYMES |
front 5 What are the properties of enzymes? | back 5 - become physically attached to the substrate - participate in bonding - do NOT become part of its products -Not used up by the chemical reaction -Can function over and over again |
front 6 Which describes energy of activation? | back 6 Minimum energy input necessary for reactants to form products in a chemical reaction - less if enzyme IS PRESENT - more if enzyme is ABSENT or low in concentration |
front 7 What are the types of enzymes? | back 7 -simple -protein alone -conjugated or holoenzyme - protein (apoenzyme) + non-protein (organic/inorganic cofactors) |
front 8 What is an apoenzyme? | back 8 -is the PROTEIN part of an enzyme -can be short or very long (100 amino acids-10^6 amino acids ) -Molecular complexity is organized 1-2-3-4 -UNIQUE ACTIVE OR CATALYTIC SITES for substrates to fit |
front 9 What is a coenzyme? | back 9 complex organic molecules, several of which come from vitamins (ex. nicotinamide, riboflavin) A DEFICIENCY in vitamins will PREVENT formation of holoenzymes affecting metabolism |
front 10 NAD | back 10 nicotinamide adenine dinucleotide (coenzyme) |
front 11 FAD | back 11 flavin adenine dinucleotide (coenzyme) |
front 12 What do coenzymes do? | back 12 Carrier of functional groups (CO2,(NH3+ = amino group NH2), and others) WORK with APOENZYME to perform necessary alterations in a substrate REMOVAL of functional groups SERVE as transient carrier of specific atoms or functional groups during metabolic reactions |
front 13 What is a cofactor? | back 13 an enzyme accessory that can be organic (coenzymes) or inorganic such as (iron, manganese, or zinc ions) Metals participate in PRECISE functions between the enzyme and the substrate ENZYMES NEED COFACTORS |
front 14 The role of cofactors are to? | back 14 ACTIVATE enzymes Help bring the active site and substrate CLOSE together Participate DIRECTLY in chemical reaction with the enzyme substrate complex |
front 15 What is the active/catalytic site? | back 15 the specific region where the substrate BINDS to the apoenzyme, or the site for reaction catalysis |
front 16 What are the steps in a chemical reaction | back 16 -Enzyme FITS substate at the active site and FORMS a complex -Bonds are FORMED BETWEEN enzyme and substrate -Reactions OCCUR on the substrate -Cofactor AIDS in the reactions -Product is FORMED AND RELEASED - Enzyme ATTACHES to another substrate molecule -Cycle repeats |
front 17 Define an exoenzyme | back 17 -extracellular action -hydrolysis -penicillases, cellulose, amylase |
front 18 Define an endoenzyme | back 18 -intracellular action -most enzymes are of this type |
front 19 What are constitutive enzymes? | back 19 enzymes that are ALWAYS present and in constant amount of cell regardless the amount of substrate |
front 20 What are properties of regulated enzymes? | back 20 - are not in constant amount in a cell -produced only when substrate is present (INDUCIBLE) -turned off when substrate is absent (REPRESSED) |
front 21 What factors can affect enzyme activity? | back 21 -temperature -pH and chemicals -osmotic pressure -heavy metals |
front 22 Describe denaturation | back 22 -occurs when weak bonds of apoenzymes are broken -distorts the shape of the enzyme -prevents the substrate from attaching to the active site |
front 23 Transfer reactions can | back 23 ADD or REMOVE functional groups |
front 24 A molecule can be | back 24 Oxidized or Reduced |
front 25 Describe oxidation | back 25 the loss or donation of electrons loss of energy |
front 26 Describe reduction | back 26 gains or accepts electrons gains energy redox reactions are COMMON in microbial cells and indispensable for life processes |
front 27 What are Oxireducatses? | back 27 A group of enzymes that can remove electrons from one substrate and add them to another |
front 28 What are the patterns of pathways | back 28 linear, cyclic, branched |
front 29 Describe competitive inhibition | back 29 other molecules with a structure similar to the normal substrate COMPETE to occupy the enzymes active site. |
front 30 What is feedback control | back 30 When the end product is being fed back into the system, cancels an enzymes activity. END PRODUCT BINDS TO AN ENZYME AND SHUTS DOWN THE PROCESS |
front 31 What are allosteric enzymes? | back 31 Enzymes that have and additional regulatory site for the attachment of molecules other than the substrate. Distort the active site so no binding to substrate occurs without denaturation |
front 32 What is enzyme repression | back 32 Excess product turns OFF genetic program in DNA |
front 33 Describe enzyme induction | back 33 -enzymes appear ONLY when suitable subtrates are present -synthesis induced by its substrate - Adaptation to the environment |
front 34 What are the properties of ATP? | back 34 -high energy molecules -STORES and RELEASES energy -unique molecular structure - a temporary energy repository -bond releases energy when broken -Negatively charged (PO4^3-) |
front 35 What is aerobic respiration? | back 35 C6H12O6+6O2 ----> 6CO2 + 6H2O + energy (ATP and HEAT) - organic compounds + oxygen ----> carbon dioxide + water +energy - glycolysis - krebs cycle (tricarboxyilic acid cycle) -Electron Transport Chain (ETC) |
front 36 Describe glycolysis | back 36 - OXIDATION of GLUCOSE into 2 MOLECULES of PYRUVIC ACID -occurs in the CYTOPLASM -most COMMONLY used sequence of reaction for the conversion of GLUCOSE into PYRUVATE - produced 2 ATP's, 2 NADH's and 2 H2O molecules -DOES NOT REQUIRE OXYGEN |
front 37 Describe the Krebs Cycle/ Tricarboxylic Acid Cycle | back 37 - discovered by egleston and krebs -occurs in the CYTOPLASM of PROKARYOTES and in the MITOCHONDRIA in EUKARYOTES -processes the final 2 acetyl-CoA coming from PYRUVIC ACID obtained from the DEGRADATION of GLUCOSE 6C though GLYCOLYSIS - cycle has 8 steps, REDUCES 2 FAD and 8 NAD's, releases 2 CO2 and PRODUCES 2 ATP by substrate level phosphoylation |
front 38 Describe the Electron Transport Chain | back 38 -occurs in the CELL MEMBRANE of PROKARYOTES and in the MITOCHONDRIA of EUKARYOTES - made of a chain of special redox carriers that recieved electrons from reduced carriers -Produces about 34 ATPS and 6 H2O MOLECULES -in aerobic metabolism, oxygen is the FINAL ELECTRON ACCEPTOR and combines with H ions (protons) to form water - in anaerobic metabolism, other ions may act as the final electron acceptors |
front 39 What is the Chemiosmotic Theory | back 39 - explains the origin and maintenance of electro-potential gradients across a membrane that leads to ATP synthase (oxidative level phosphorylation) - the energy obtained is used to GENERATE up to 38 ATP |
front 40 Describe Anaerobic Respiration | back 40 -fermentation - the conversion of PYRUVIC ACID to ORGANIC ACID or alcohol (or other organic compounds, producing ATP -organic molecules can serve as FINAL ELECTRON ACCEPTORS - 2 ATP's maximum per glucose molecule |
front 41 What is a Fermentor | back 41 A large tank used in industrial microbiology to grow mass quantities of microbes that can synthesize desired products - equipped with the means to stir, monitor, and harvest products such as a variety of organic acids and alcohols in very large quanities |
front 42 What is Amphibolism? | back 42 the property of a system to integrate catabolic and anabolic pathways to improve cell efficiency |
front 43 Describe Amination | back 43 when pyruvic acid can be CONVERTED to amino acids by adding NH4+ |
front 44 Transamination is | back 44 when an amino acid and a carbohydrate make another amino acid |
front 45 Deamination is | back 45 when amino acids can be used as a SOURCE OF GLUCOSE (glucogenisis) releasing NH4+ |
front 46 When an enzyme is inducive it means | back 46 it wants to add more, when a substrate is present |
front 47 Allosteric inhibition is | back 47 when inhibitor BINDS to holoenzyme and CHANGES the shape; making the substrate unable to bind |
front 48 exergonic is | back 48 a reaction that releases energy as it proceeds forward |
front 49 endergonic is | back 49 reactions that proceed when energy is added |
front 50 Cellular respiration is | back 50 O2 + organic molecule Chloroplast take CO2 + H2O ----> glucose + oxygen |
front 51 What is the name of the 3-carbon molecule produced in glycolysis? | back 51 pyruvic acid |
front 52 what are the two MAIN products of aerobic respiration? | back 52 ATP and WATER |
front 53 Name of the two carbon molecule that feed or enters directly into the krebs cycle | back 53 Acetyl-CoA |
front 54 how many ATP's are produced from a glucose molecule in bacteria? | back 54 38 |