Biochemistry Flashcards

4559501411	coenzyme	A non-protein substance that takes part in an enzymatic reaction and is regenerated for further reaction	0
4559502496	Stays the same.	Competitive inhibitor on vmax?	1
4559505466	Specific rate constant	A constant relating molar concentration of reactants to race of reaction (k)	2
4559510192	Reaction reaches equilibrium	The 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	#6	DNA Ligase	4
4559512426	Allosteric	Other shape	5
4559516945	a 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
4559518988	Entropy	randomness/disorder?	7
4559521400	Stage 2 metabolism	The initial oxidation of carbon to yield intermediated than can be further oxidised?	8
4559522819	Glycogen	Major energy storage carbohydrate?	9
4559524328	Hylauric acid	Glycosoaminoglucan found in human joints?	10
4559525128	Epimers	Glucose and galactose are?	11
4559527068	No as they dont contain glycosidic bonds.	Can glycosidic bond hydrolysis happen for a monosaccharise?	12
4559529969	glyceraldehyde-3-phosphate----> 1,3 biphosphoglycerate	What step in glycolysis results in oxidation	13
4559536193	triosephosphate	What is not a point of regulation in glycolysis?	14
4559538235	Glucose-6-phosphate	What inhibits glycolysis?	15
4559539158	No	Is ethanol a precursor to make glucose?	16
4559540208	ATP	What inhibits pyruvate kinase?	17
4559543000	No	IS cholesterol a biosynthetic precursor for CoA	18
4559544730	Maximal velocity when enzyme is fully saturated.	vmax?	19
4559546284	Michaelas constant defined as concentration of s at which v=1/2max. Affinity.	Km?	20
4559558039	To see how fast forward reaction is going without affect of the back reaction.	measure velocity at the start?	21
4559565115	Adipose tissue.	Where are fats stored?	22
4559567074	Lower the melting point.	The greater the degree of unsaturation the?	23
4559575464	If an enzyme is active or inactive.	Phosphorylation regulates?	24
4559588933	Transition state	In an enzymatic reaction what does ES represent?	25
4559591264	Give an alternative reaction path, lowering the activation energy.	Enzymes work by?	26
4559594981	Vinit = Vmax[s]/Km+ [s]	Michaelis-Menten Equation?	27
4559598329	Biological catalyst.	Enzyme is?	28
4559600927	Vmax Decreases and Km stays the same.	Change in Km and Vmax in presence of a non-competitive inhibitor.	29
4559602659	Vmad stays the same, Km increases.	Change in Km and Vmax in competitive inhibition?	30
4559607110	increase as fatty acid chain length increases, decrease as fatty acid unsaturation decreases.	The transition temperature of a lipid bilayer membrane will	31
4559612273	Oxaloacetate	What alpha-keto acid corresponds with the amino acid aspartate?	32
4559616768	Glutamate	Ammonia can be incorporated directly into an alpha-keto acid by reductive amination to yield what amino acid?	33
4559621088	Aspartate transaminase.	What enzyme is not used in aneuplerotic reations that convert carbohydrates to citric acid cycle intermediates	34
4559623932	succinyl-CoA Synthase.	The only reaction of the TCA cycle which provides substrate-level phosphorylation is catalysed by?	35
4559626596	Inhibited: Acetyl-CoA, NADH, ATP and FA Activated by: AMP, CoA, NAD+, Ca2+	Pyruvate dehydrogenase inhibited and activated by	36
4559630405	Inhibited: Increased ATP, citrate, succinyl-CoA and NADH Activated by: ADP	Citrate synthase activated and inhibited by	37
4559632755	Activated by: ADP and Ca2+ Inhibited by: NADH and ATP	Isocitrate Dehydrogenase activation and inhibition	38
4559636737	Inhibited by: succinyl-CoA and NADH Activated by: Ca2+	alpha-keto glutarate activation and inhibition	39
4559641101	NADH	Malate dehydrogenase inhibited by?	40
4596445185	Produced when oxaloacetate is in insufficient supply and when carbohydrate metabolism lags behind lipid metabolism	Under what conditions are ketone bodies produced?	41
4596447253	Proline	Which of the standard 20 amino acids is technically not an amino acid?	42
4596447607	Glycine	Which of the standard 20 amino acids contains no chiral carbon?	43
4596449762	4	How many ATP-equivalents are required for one round of the urea cycle?	44
4596450615	To reduce the concentration of urea in the urine	People on high protein diets are advised to drink lots of water. Why?	45
4596452384	Mitochondria	The citric acid cycle takes place in the ...?	46
4596453010	Cytosol	Glycolysis takes place in the ...?	47
4596458179	All of them contain heme groups	What unusual property do cytochromes have in common with hemoglobin or myoglobin?	48
4596461890	The hydrophobic interaction among the hydrocarbon tails of the phospholipids.	What is the main energetic driving force for the formation of phospholipid bilayers?	49
4600322842	Stage 1	Proteins, polysaccharides, and lipids are broken down into their component building blocks. What stage of catabolism?	50
4600324306	Stage 2	The building blocks are degraded into the common product, the acetyl groups of acetyl-CoA. What stage of catabolism?	51
4600326872	3	Catabolism converges to three principal end products: water, carbon dioxide, and ammonia. Stage?	52
4600351110	Energy change when reaction proceeds from start to equilibrium	Gibbs Free Energy is?	53
4600358381	Negative	Energy is Released, Reaction is Exergonic & will favour the formation of products when Gibbs free energy is?	54
4600363590	Positive	Energy is Absorbed, Reaction is Endergonic & will favour the formation of reactants when gibbs free energy is?	55
4600390963	electrons are transferred from a donor to an acceptor	Oxidation-Reduction reactions are those in which	56
4600396601	Catabolism	the transfer of electrons to acceptor molecules of various sorts happens in?	57
4600403503	Anabolism	Process involving the acceptance of electrons from a variety of donors is?	58
4600424044	nicotinamide ring, adenine ring and 2 sugar phosphate groups	NAD+/NADH contains?	59
4600428046	In the nicotinamide ring	Where does reduction/oxidation occur on NAD+?	60
4600432613	NAD+/NADH and FAD/FADH	Biological oxidising agents include?	61
4600437840	require/release convenient amount of energy, depending on direction of reaction.	High energy bonds are bonds that?	62
4600446077	Formation of a more reactive substance	What is activation in metabolism?	63
4600458255	Provides an alternative pathway with a lower activation energy.	What does an enzyme do?	64
4600466896	catalyse a redox reaction (#1)	oxidoreductases?	65
4600467671	Transfer a functional group (#2)	Tranferases?	66
4600469165	cause hydrolysis reaction(#3)	Hydrolases	67
4600471205	break bonds (#4)	lyases	68
4600473115	Rearrange functional groups (#5)	isomerases?	69
4600474150	Join two molecules (#6)	Ligases?	70
4600486867	1. 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 state	Steps in enzymatic reaction?	71
4600511740	Difference in energies between initial state and final state	Change in free energy is	72
4600515769	change in free energy and equilibrium constant		73
4600524870	The selective hydrolysis of peptide bonds where the carboxyl is contributed by Phe and Tyr and hydrolysis of ester bonds.	Chymotrypsin catalyses?	74
4600531664	Rate depends on concentration of substrate	First order kinetics?	75
4600533167	Rate does not depend on concentration of substrate	Zero-order kinetics?	76
4600561758	Number of moles of substrate that react to form product per mole of enzyme per unit of time	Kcat is?	77
4600568553	an inactive precursor into an active enzyme	phosphorylation of ATP can convert?	78
4600570968	Inactive precursor of an enzyme where cleavage of one or more covalent bonds transform it into an active enzyme	Zymogen?	79
4600580849	When the final product of a reaction blocks an early reaction and shuts down whole series.	What is feedback inhibition?	80
4600595413	K System: Alters K0.5 V system: alters Vmax.	Two types of allosteric enzyme systems, what are they and what do they effect?	81
4600697062	one that reducing an oxidising agent	Whats a reducing sugar?	82
4600701592	an amino sugar	The replacement of a hydroxyl group on a carbohydrate results in	83
4600709094	by transfer of a phosphate group from ATP	phosphoric esters are formed?	84
4600711768	a carbohydrate in which the -OH of the anomeric carbon is replaced by -OR	Glycoside?	85
4600738816	continuous, unbranched chains of up to 4000 a-D-glucose units joined by -1,4-glycosidic bonds	amylose	86
4600740390	a highly branched polymer consisting of 24-30 units of D-glucose joined by -1,4-glycosidic bonds and branches created by -1,6-glycosidic bonds	amylopectin	87
4600745448	polysaccharides 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 group	Glycosaminoglycans	88
4600747387	natural anticoagulant	heparin	89
4600749961	a component of the vitreous humor of the eye and the lubricating fluid of joints	Hyaluronic acid	90
4600757777	energy-storage polymers or sugars	Starch and glycogen are	91
4600759074	are structural polymers	Cellulose and chitin	92
4600761248	contain carbohydrate units covalently bonded to a polypeptide chain	Glycoproteins	93
4600763001	antibodies	An example of a glycoprotein?	94
4600767113	dense carbohydrate layer around some cells.	Glycocalix	95
4600768563	Are proteins that bind carbohydrates with high specificity and affinity.	Lectins?	96
4600774314	Long filaments of derivatised glucose disaccharides, Major component of cartilage and connective tissues, including dental pulp	proteoglycans	97
4601341101	hexokinase, 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
4601349828	Reduction of pyruvate to lactate	Under anaerobic conditions, the most important pathway for the regeneration of NAD+ is	99
4601372181	Fructose-2,6-Bisphosphate: produced in liver in response to insulin	is an important regulator of blood glucose	100
4601375225	gluconeogenesis	low fructose-2,6-biphosphate stimulates	101
4601376709	glycolysis.	high fructose-2,6-biphosphate stimulates	102
4601378747	when 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 glucose	what is the cori cycle	103
4601383862	Allosteric effects, genetic control, subtrate cycles and covalent modification	the four control mechanisms in carbohydrate metabolism are?	104
4601385861	effectors of a pathway inhibit or activate an enzyme	Allosteric effects control is?	105
4601388193	amount of enzymes present are increased by protein synthesis.	Genetic control?	106
4601389395	Inhibition or activation of an enzyme is controlled by the breaking or joining of a bond by being phophorylated or dephosphorylated.	Covalent modification	107
4601391905	two opposing reactions are catalysed by different enzymes seperately.	Substrate cycle?	108
4601401354	Undergo hydrolytic cleavage into smaller compounds in the presence of acid, base or digestive enzymes, e.g. triacylglycerols, waxes, glycerophospholipids, and sphingolipids	Hydrolyzable lipids are?	109
4601402905	do not undergo hydrolytic cleavage, e.g. steroids, eicosanoids and fat soluble vitamins	Non-hydrolyzable lipids:	110
4601404944	an unbranched-chain carboxylic acid, most commonly of 12 - 20 carbons, derived from hydrolysis of animal fats, vegetable oils, or phosphodiacylglycerols of biological membranes	Fatty acid	111
4601409818	Unsaturated	double bonds make fatty acids?	112
4601410840	Lower the melting point	the greater the degree of unsaturation in FA the?	113
4601412808	number of carbons increase and number of double bonds increase	Melting point of FA increases as? and decreases as?	114
4601419080	a compound in which a carbohydrate is bound to an -OH of the lipid	Glycolipid	115
4601435166	Phospholipids	lipid bilayers composed mainly of?	116
4601437155	transport substances across membranes; act as receptor sites, and sites of enzyme catalysis	Function of membrane proteins?	117
4601439626	Lysosomes are organelles surrounded by a single membrane and filled with enzymes, such as acid hydrolases, that degrade a variety of macromolecules.	Lysosomes	118
4601441202	transport is linked to the hydrolysis of ATP or other high-energy molecules (Na/K ion pump)	Primary active transport	119
4601443112	driven by H+ gradient	Secondary active transport	120
4601446482	Hormone binding to its cell surface receptor transduces information via activated heterotrimeric G-protein and cAMP	Plasma membrane receptors	121
4601447386	oxidation will yeild more energy and they can pack more tightly in stored tissues.	2 major advantages for storing energy as fat?	122
4601458723	Dietary triacylglycerols Triacylglycerols synthesized in the liver Triacylglycerols stored in fat cells.	3 primary sources of fatty acids	123
4601496999	liver, heart and skeletal muscles.	Where does beta oxidation occur?	124
4601505313	Emulsification	what process breaks up lipid droplets?	125
4601511831	micelles bump into the brush border and the monoglycerides and fatty acids are liberated and absorbed	what do miscelles (formed from bile salts) do?	126
4601518899	Fat transport vehicles	lipoproteins are?	127
4601519678	Chylomicrons - 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 excretion	4 main types of lipoproteins?	128
4601525106	adipocytes, myocytes and liver cells	lipids are absorbed into?	129
4601526223	It is linked to the endothelial cell surface by a polysaccharide chain and anchors the chylomicron to the capillary surface.	Lipoprotein lipase?	130
4601529333	Apoprotein C-11	What activates lipoprotein lipase?	131
4601530140	Hydrolysed to glycerol and fats	The triglycerides from chylomicrons and VLDL are	132
4601553659	Presence of cholesterol in cel	What regulates LDL?	133
4601561475	Oxidation of FA in tiacylglycerols.	What is the principal storage form of energy for most organisms?	134
4601562799	hydrolysis of bonds between fatty acids and the rest of triacylglycerols.	Lipases catalyse?	135
4601564347	hydrolysis of bonds between fatty acids and the rest of the phophoglycerol	Phopholipases catalyse?	136
4601608508	Glycerol-3-phophate, dihydroxyacetone phophate and diacylglycerol	What are the three pathways phophatidic acid is produced in?	137
4601610600	isoprene	What is the key to the biosynthesis of steroids?	138
4601629235	when the amount of acetyl-CoA produced is excessive compared to the amount of oxaloacetate available to react with it	When does formation of ketone bodies occur?	139
4601629538	acetone, -hydroxybutyrate, and acetoacetate	Ketone bodies consist of?	140
4605126312	Small intracellular organelles that absorb and degrade damaged proteins.	Lysosomes are?	141
4605132951	Large MW complex which breaks down proteins, binds to uniquinated proteins	Proteosomes?	142
4605137458	Ubiquitin targets intracellular proteins for degradation by covalently binding to the ε-amino group of lysine residues. Releases short peptides into cytoplasm	What are ubiquinated proteins?	143
4605164242	Too much protein is ingested Starvation Diabetes	Amino acids are used as fuel when?	144
4605166111	Via the citric acid cycle	How are amino acids oxidised?	145
4605172530	True	the fate of the carbons of the amino acids parallels that of glucose and fatty acids. True or false	146
4605176751	transamination	What is the major process for removing nitrogen from amino acids?	147
4605180317	lysine and threonine	What amino acids dont undergo transamination reaction?	148
4605185415	amino transferase moves the amino group to alpha-ketoglutarate producing glutarate or to oxaloacetate producing aspartate	Transamination reaction?	149
4605191664	Removal of amino group from glutamate producing an ammonium ion.	Oxidative deamination?	150
4605206968	active form of B6 and participates in the catalysis of transaminations and decarboxylations	What does pyridoxal phosphate do?	151
4605233653	hydrolysed to amino acids in gut by intestinal proteases	proteins ingested in diet are?	152
4605262792	reduction of N2 to NH3	What is nitrogen fixation?	153
4605265269	The nitrogenase enzyme found in root nodules of leguminous plants	What catalyzes crucial reactions in nitrogen fixation.	154
4605268079	Histidine, triptophan, AMP and CTP	Glutamine synthetase is feedback inhibited by several end products, what are they?	155
4605275511	produced by plants and bacteria	What is an essential amino acid?	156
4605276664	those that can be produced by animals	What is a non-essential amino acid?	157
4605283285	biotin, SAM, and derivatives of folic acid	What are the carriers of one carbond groups?	158
4605290673		What is phagocytosis and autophagy	159
4605299159	folate (Vitamin B9)	tetrahydrofolate is derived from	160
4605300422	Methionine	S-adenosylmethionine is derived from	161