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Biochemistry Flashcards

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4559501411coenzymeA non-protein substance that takes part in an enzymatic reaction and is regenerated for further reaction0
4559502496Stays the same.Competitive inhibitor on vmax?1
4559505466Specific rate constantA constant relating molar concentration of reactants to race of reaction (k)2
4559510192Reaction reaches equilibriumThe velocity of the forward reactiion to form c and d would be equal to that of the reverse reaction for a and b in a strongly exergonic chemical reaction when?3
4559512425#6DNA Ligase4
4559512426AllostericOther shape5
4559516945a product of another enzyme in the same metabolic pathway as the inhibited enzyme.When a molecule binds reversibly to an enzyme and mediated feedback inhibition, the inhibitory molecule would most likely be?6
4559518988Entropyrandomness/disorder?7
4559521400Stage 2 metabolismThe initial oxidation of carbon to yield intermediated than can be further oxidised?8
4559522819GlycogenMajor energy storage carbohydrate?9
4559524328Hylauric acidGlycosoaminoglucan found in human joints?10
4559525128EpimersGlucose and galactose are?11
4559527068No as they dont contain glycosidic bonds.Can glycosidic bond hydrolysis happen for a monosaccharise?12
4559529969glyceraldehyde-3-phosphate----> 1,3 biphosphoglycerateWhat step in glycolysis results in oxidation13
4559536193triosephosphateWhat is not a point of regulation in glycolysis?14
4559538235Glucose-6-phosphateWhat inhibits glycolysis?15
4559539158NoIs ethanol a precursor to make glucose?16
4559540208ATPWhat inhibits pyruvate kinase?17
4559543000NoIS cholesterol a biosynthetic precursor for CoA18
4559544730Maximal velocity when enzyme is fully saturated.vmax?19
4559546284Michaelas constant defined as concentration of s at which v=1/2max. Affinity.Km?20
4559558039To see how fast forward reaction is going without affect of the back reaction.measure velocity at the start?21
4559565115Adipose tissue.Where are fats stored?22
4559567074Lower the melting point.The greater the degree of unsaturation the?23
4559575464If an enzyme is active or inactive.Phosphorylation regulates?24
4559588933Transition stateIn an enzymatic reaction what does ES represent?25
4559591264Give an alternative reaction path, lowering the activation energy.Enzymes work by?26
4559594981Vinit = Vmax[s]/Km+ [s]Michaelis-Menten Equation?27
4559598329Biological catalyst.Enzyme is?28
4559600927Vmax Decreases and Km stays the same.Change in Km and Vmax in presence of a non-competitive inhibitor.29
4559602659Vmad stays the same, Km increases.Change in Km and Vmax in competitive inhibition?30
4559607110increase as fatty acid chain length increases, decrease as fatty acid unsaturation decreases.The transition temperature of a lipid bilayer membrane will31
4559612273OxaloacetateWhat alpha-keto acid corresponds with the amino acid aspartate?32
4559616768GlutamateAmmonia can be incorporated directly into an alpha-keto acid by reductive amination to yield what amino acid?33
4559621088Aspartate transaminase.What enzyme is not used in aneuplerotic reations that convert carbohydrates to citric acid cycle intermediates34
4559623932succinyl-CoA Synthase.The only reaction of the TCA cycle which provides substrate-level phosphorylation is catalysed by?35
4559626596Inhibited: Acetyl-CoA, NADH, ATP and FA Activated by: AMP, CoA, NAD+, Ca2+Pyruvate dehydrogenase inhibited and activated by36
4559630405Inhibited: Increased ATP, citrate, succinyl-CoA and NADH Activated by: ADPCitrate synthase activated and inhibited by37
4559632755Activated by: ADP and Ca2+ Inhibited by: NADH and ATPIsocitrate Dehydrogenase activation and inhibition38
4559636737Inhibited by: succinyl-CoA and NADH Activated by: Ca2+alpha-keto glutarate activation and inhibition39
4559641101NADHMalate dehydrogenase inhibited by?40
4596445185Produced when oxaloacetate is in insufficient supply and when carbohydrate metabolism lags behind lipid metabolismUnder what conditions are ketone bodies produced?41
4596447253ProlineWhich of the standard 20 amino acids is technically not an amino acid?42
4596447607GlycineWhich of the standard 20 amino acids contains no chiral carbon?43
45964497624How many ATP-equivalents are required for one round of the urea cycle?44
4596450615To reduce the concentration of urea in the urinePeople on high protein diets are advised to drink lots of water. Why?45
4596452384MitochondriaThe citric acid cycle takes place in the ...?46
4596453010CytosolGlycolysis takes place in the ...?47
4596458179All of them contain heme groupsWhat unusual property do cytochromes have in common with hemoglobin or myoglobin?48
4596461890The hydrophobic interaction among the hydrocarbon tails of the phospholipids.What is the main energetic driving force for the formation of phospholipid bilayers?49
4600322842Stage 1Proteins, polysaccharides, and lipids are broken down into their component building blocks. What stage of catabolism?50
4600324306Stage 2The building blocks are degraded into the common product, the acetyl groups of acetyl-CoA. What stage of catabolism?51
46003268723Catabolism converges to three principal end products: water, carbon dioxide, and ammonia. Stage?52
4600351110Energy change when reaction proceeds from start to equilibriumGibbs Free Energy is?53
4600358381NegativeEnergy is Released , Reaction is Exergonic & will favour the formation of products when Gibbs free energy is?54
4600363590PositiveEnergy is Absorbed , Reaction is Endergonic & will favour the formation of reactants when gibbs free energy is?55
4600390963electrons are transferred from a donor to an acceptorOxidation-Reduction reactions are those in which56
4600396601Catabolismthe transfer of electrons to acceptor molecules of various sorts happens in?57
4600403503AnabolismProcess involving the acceptance of electrons from a variety of donors is?58
4600424044nicotinamide ring, adenine ring and 2 sugar phosphate groupsNAD+/NADH contains?59
4600428046In the nicotinamide ringWhere does reduction/oxidation occur on NAD+?60
4600432613NAD+/NADH and FAD/FADHBiological oxidising agents include?61
4600437840require/release convenient amount of energy, depending on direction of reaction.High energy bonds are bonds that?62
4600446077Formation of a more reactive substanceWhat is activation in metabolism?63
4600458255Provides an alternative pathway with a lower activation energy.What does an enzyme do?64
4600466896catalyse a redox reaction (#1)oxidoreductases?65
4600467671Transfer a functional group (#2)Tranferases?66
4600469165cause hydrolysis reaction(#3)Hydrolases67
4600471205break bonds (#4)lyases68
4600473115Rearrange functional groups (#5)isomerases?69
4600474150Join two molecules (#6)Ligases?70
46004868671. Enzyme binds substrate at the active site to form an enzyme-substrate complex (ES) 2. Binding lowers activation energy 3. The ES complex goes through transition state ES* (Not quite substrate or product) 4. Specific R group plays a role in the catalysis 5. Enzyme undergoes conformational change 6. Complex of enzyme and product are produced (EP) 7. Enzyme and product separate 8. Enzyme recycles to original stateSteps in enzymatic reaction?71
4600511740Difference in energies between initial state and final stateChange in free energy is72
4600515769change in free energy and equilibrium constant73
4600524870The selective hydrolysis of peptide bonds where the carboxyl is contributed by Phe and Tyr and hydrolysis of ester bonds.Chymotrypsin catalyses?74
4600531664Rate depends on concentration of substrateFirst order kinetics?75
4600533167Rate does not depend on concentration of substrateZero-order kinetics?76
4600561758Number of moles of substrate that react to form product per mole of enzyme per unit of timeKcat is?77
4600568553an inactive precursor into an active enzymephosphorylation of ATP can convert?78
4600570968Inactive precursor of an enzyme where cleavage of one or more covalent bonds transform it into an active enzymeZymogen?79
4600580849When the final product of a reaction blocks an early reaction and shuts down whole series.What is feedback inhibition?80
4600595413K System: Alters K0.5 V system: alters Vmax.Two types of allosteric enzyme systems, what are they and what do they effect?81
4600697062one that reducing an oxidising agentWhats a reducing sugar?82
4600701592an amino sugarThe replacement of a hydroxyl group on a carbohydrate results in83
4600709094by transfer of a phosphate group from ATPphosphoric esters are formed?84
4600711768a carbohydrate in which the -OH of the anomeric carbon is replaced by -ORGlycoside?85
4600738816continuous, unbranched chains of up to 4000 a-D-glucose units joined by -1,4-glycosidic bondsamylose86
4600740390a highly branched polymer consisting of 24-30 units of D-glucose joined by -1,4-glycosidic bonds and branches created by -1,6-glycosidic bondsamylopectin87
4600745448polysaccharides based on a repeating disaccharide where one of the monomers is an amino sugar and the other has a negative charge due to a sulfate or carboxylate groupGlycosaminoglycans88
4600747387natural anticoagulantheparin89
4600749961a component of the vitreous humor of the eye and the lubricating fluid of jointsHyaluronic acid90
4600757777energy-storage polymers or sugarsStarch and glycogen are91
4600759074are structural polymersCellulose and chitin92
4600761248contain carbohydrate units covalently bonded to a polypeptide chainGlycoproteins93
4600763001antibodiesAn example of a glycoprotein?94
4600767113dense carbohydrate layer around some cells.Glycocalix95
4600768563Are proteins that bind carbohydrates with high specificity and affinity.Lectins?96
4600774314Long filaments of derivatised glucose disaccharides, Major component of cartilage and connective tissues, including dental pulpproteoglycans97
4601341101hexokinase, phosphofructokinase and pyruvate kinase.the three enzyme that exhibit large decreases of free energy and are a site of allosteric control in glycolysis are?98
4601349828Reduction of pyruvate to lactateUnder anaerobic conditions, the most important pathway for the regeneration of NAD+ is99
4601372181Fructose-2,6-Bisphosphate: produced in liver in response to insulinis an important regulator of blood glucose100
4601375225gluconeogenesislow fructose-2,6-biphosphate stimulates101
4601376709glycolysis.high fructose-2,6-biphosphate stimulates102
4601378747when different organisms share carbohydrate metabolism. Example: liver shares stress of vigorous exercise. Lactate from muscle is transported to the liver where it is reoxidized to pyruvate and converted to glucosewhat is the cori cycle103
4601383862Allosteric effects, genetic control, subtrate cycles and covalent modificationthe four control mechanisms in carbohydrate metabolism are?104
4601385861effectors of a pathway inhibit or activate an enzymeAllosteric effects control is?105
4601388193amount of enzymes present are increased by protein synthesis.Genetic control?106
4601389395Inhibition or activation of an enzyme is controlled by the breaking or joining of a bond by being phophorylated or dephosphorylated.Covalent modification107
4601391905two opposing reactions are catalysed by different enzymes seperately.Substrate cycle?108
4601401354Undergo hydrolytic cleavage into smaller compounds in the presence of acid, base or digestive enzymes, e.g. triacylglycerols, waxes, glycerophospholipids, and sphingolipidsHydrolyzable lipids are?109
4601402905do not undergo hydrolytic cleavage, e.g. steroids, eicosanoids and fat soluble vitaminsNon-hydrolyzable lipids:110
4601404944an unbranched-chain carboxylic acid, most commonly of 12 - 20 carbons, derived from hydrolysis of animal fats, vegetable oils, or phosphodiacylglycerols of biological membranesFatty acid111
4601409818Unsaturateddouble bonds make fatty acids?112
4601410840Lower the melting pointthe greater the degree of unsaturation in FA the?113
4601412808number of carbons increase and number of double bonds increaseMelting point of FA increases as? and decreases as?114
4601419080a compound in which a carbohydrate is bound to an -OH of the lipidGlycolipid115
4601435166Phospholipidslipid bilayers composed mainly of?116
4601437155transport substances across membranes; act as receptor sites, and sites of enzyme catalysisFunction of membrane proteins?117
4601439626Lysosomes are organelles surrounded by a single membrane and filled with enzymes, such as acid hydrolases, that degrade a variety of macromolecules.Lysosomes118
4601441202transport is linked to the hydrolysis of ATP or other high-energy molecules (Na/K ion pump)Primary active transport119
4601443112driven by H+ gradientSecondary active transport120
4601446482Hormone binding to its cell surface receptor transduces information via activated heterotrimeric G-protein and cAMPPlasma membrane receptors121
4601447386oxidation will yeild more energy and they can pack more tightly in stored tissues.2 major advantages for storing energy as fat?122
4601458723Dietary triacylglycerols Triacylglycerols synthesized in the liver Triacylglycerols stored in fat cells.3 primary sources of fatty acids123
4601496999liver, heart and skeletal muscles.Where does beta oxidation occur?124
4601505313Emulsificationwhat process breaks up lipid droplets?125
4601511831micelles bump into the brush border and the monoglycerides and fatty acids are liberated and absorbedwhat do miscelles (formed from bile salts) do?126
4601518899Fat transport vehicleslipoproteins are?127
4601519678Chylomicrons - carry dietary fats to peripheral tissues VLDL - carry tg and other lipids made in liver to body LDL - principle form for cholesterol transport HDL - scavenges excess cholesterol from tissues and returns to liver for metabolism and excretion4 main types of lipoproteins?128
4601525106adipocytes, myocytes and liver cellslipids are absorbed into?129
4601526223It is linked to the endothelial cell surface by a polysaccharide chain and anchors the chylomicron to the capillary surface.Lipoprotein lipase?130
4601529333Apoprotein C-11What activates lipoprotein lipase?131
4601530140Hydrolysed to glycerol and fatsThe triglycerides from chylomicrons and VLDL are132
4601553659Presence of cholesterol in celWhat regulates LDL?133
4601561475Oxidation of FA in tiacylglycerols.What is the principal storage form of energy for most organisms?134
4601562799hydrolysis of bonds between fatty acids and the rest of triacylglycerols.Lipases catalyse?135
4601564347hydrolysis of bonds between fatty acids and the rest of the phophoglycerolPhopholipases catalyse?136
4601608508Glycerol-3-phophate, dihydroxyacetone phophate and diacylglycerolWhat are the three pathways phophatidic acid is produced in?137
4601610600isopreneWhat is the key to the biosynthesis of steroids?138
4601629235when the amount of acetyl-CoA produced is excessive compared to the amount of oxaloacetate available to react with itWhen does formation of ketone bodies occur?139
4601629538acetone, -hydroxybutyrate, and acetoacetateKetone bodies consist of?140
4605126312Small intracellular organelles that absorb and degrade damaged proteins.Lysosomes are?141
4605132951Large MW complex which breaks down proteins, binds to uniquinated proteinsProteosomes?142
4605137458Ubiquitin targets intracellular proteins for degradation by covalently binding to the ε-amino group of lysine residues. Releases short peptides into cytoplasmWhat are ubiquinated proteins?143
4605164242Too much protein is ingested Starvation DiabetesAmino acids are used as fuel when?144
4605166111Via the citric acid cycleHow are amino acids oxidised?145
4605172530Truethe fate of the carbons of the amino acids parallels that of glucose and fatty acids. True or false146
4605176751transaminationWhat is the major process for removing nitrogen from amino acids?147
4605180317lysine and threonineWhat amino acids dont undergo transamination reaction?148
4605185415amino transferase moves the amino group to alpha-ketoglutarate producing glutarate or to oxaloacetate producing aspartateTransamination reaction?149
4605191664Removal of amino group from glutamate producing an ammonium ion.Oxidative deamination?150
4605206968active form of B6 and participates in the catalysis of transaminations and decarboxylationsWhat does pyridoxal phosphate do?151
4605233653hydrolysed to amino acids in gut by intestinal proteasesproteins ingested in diet are?152
4605262792reduction of N2 to NH3What is nitrogen fixation?153
4605265269The nitrogenase enzyme found in root nodules of leguminous plantsWhat catalyzes crucial reactions in nitrogen fixation.154
4605268079Histidine, triptophan, AMP and CTPGlutamine synthetase is feedback inhibited by several end products, what are they?155
4605275511produced by plants and bacteriaWhat is an essential amino acid?156
4605276664those that can be produced by animalsWhat is a non-essential amino acid?157
4605283285biotin, SAM, and derivatives of folic acidWhat are the carriers of one carbond groups?158
4605290673What is phagocytosis and autophagy159
4605299159folate (Vitamin B9)tetrahydrofolate is derived from160
4605300422MethionineS-adenosylmethionine is derived from161

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