Biochemistry Flashcards

9195656026	Enzymes alter	reaction rate, equilibrium	0
9195687991	free energy of peptide bond is	exergonic (release)	1
9195752131	exergonic -ΔG is	spontaneous	2
9195757411	endergonic +ΔG is	non-spontaneous	3
9195847666	decreasing ΔG will	accelerate reactions	4
9195867941	hydrolysis of pb is exergonic and moves slow	high activation energy	5
9195871454	active site of an enzyme is	the location where the substrate binds	6
9195906866	chemical complementarity	has proper shape and stereochemistry ahead of time to allow binding of the substrate and stabilization by non-covalent interactions with r-groups	7
9195943253	lock and key model	complementarity before substrate binding	8
9195947074	induced fit model	enzyme adjusts to form complementarity after substrate binding	9
9195951743	catalytic triad	Ser195, His52, Asp102	10
9195959187	Chymotrypsin cleaves	pb after bulky or aromatic (phenylalanine or tryosine)	11
9195963066	Trypsin cleaves	pb that are basic and negatively charged (lysine and arginine)	12
9195969300	elastase cleaves	pb with small side chains (glycine, alanine, valine)	13
9195998000	serine proteases	have catalytic triad, covalent intermediate	14
9196002034	aspartate proteases	two asp residues, direct nucleophilic attack by water	15
9196012220	aspartic acid is	the acid residue	16
9196014292	histidine	polarizes or aligns the base	17
9196016392	serine	activates the nucleophile	18
9196022800	covalent catalysis (chymotrypsin)	form intermediate and breakdown the intermediate	19
9196027159	purpose of the catalytic triad	speed up rxn in proteases	20
9196035719	oxyanion hole	stabilizes transition state from its positively charged residues	21
9196046290	s1 pocket	specificity, hydrophobic residues	22
9196057561	allosteric enzymes	proteins that alter the shape and activity with bonding of allosteric effector at allosteric site	23
9196070251	allosteric effector	change the shape of the enzyme allowing it bind with substrate	24
9196076688	allosteric site is	placed on an enzyme where a molecule that is not a substrate may bind	25
9196088218	allosteric enzymes do not	follow michaelis-menten kinetics bc more than two active sites and subunits	26
9196096227	regulate ATCase bc	it catalyzes the first step in pyrimidine biosynthesis, if not there rxn will use all of its energy up trying to synthesize pyrimidines	27
9196108338	ATCase has	six catalytic and six regulatory subunits	28
9196116717	PALA is	a competitive inhibitor that binds at the active site of ATCase	29
9196131485	when PALA binds to catalytic triad this state is favored	R	30
9196136137	in the absence of substrates this state is favored	T	31
9196142485	T state is stabilized by	CTP binding to an allosteric site on the regulatory subunit	32
9196153120	Phosphorylation is a good mechanism to	alter the structure and function of proteins bc its reversible	33
9196159732	protein kinase A has	two catalytic and two regulatory subunits	34
9196168056	Protein Kinase A is activated by	cyclic AMP (weakens R and C interactions to open up active sites for binding)	35
9196177073	Vmax is	max velocity at which the enzyme catalyzes a rxn	36
9196182426	Km is the	substrate concentration at 1/2 vmax	37
9196186030	An enzyme with Km has a low	affinity and needs higher [S] to get to vmax	38
9196195919	enzymes reduce ΔG	low free energy of ts by binding to it tightly, changing reaction pathway	39
9196205389	Michaelis-Menten Equation		40
9196221191	Km does not	depend on [e]	41
9196248029	glucose haworth		42
9196254507	glucose chair		43
9196270952	glucose fischer		44
9196274391	mannose chair		45
9196278524	mannose fischer		46
9196284061	mannose haworth		47
9196288870	galactose chair		48
9196302036	galactose haworth		49
9196311616	galactose fischer		50
9196319200	glycosidic bonds are	anhydrous covalent links between an alcohol and the anomeric oh of a sugar. reducing properties are lost	51
9196328269	in n link glycosylation	the sugar is attached through a nitrogen (asparagine or arginine)	52
9196333818	in o linked glycosylation	the sugar is attached through a oxygen on a oh group (serine, threonine, or tyrosine)	53
9196346802	fructose fischer		54
9196350817	fructose haworth		55
9196369170	reducing sugars contain a	hemiacetal	56
9196369172	hemiacetals have	one oh group and one or group attached	57
9196382960	pump goes through	active transport, across membrane against the gradient	58
9196386397	channel ions	go through passive transport	59
9196395469	membrane fluidity is controlled by	temperature, amount of cholesterol, and stereolipids	60
9196405938	where fatty acids are extended (low motion and lateral diffusion)	paracrystalline gel phase	61
9196411362	enzyme exists in two conformational states	E1 and E2	62
9196411363	E is the	resting state with two Ca2+	63
9196416323	Atp bind to the	domain and is hydrolyzed	64
9196422006	Adp is released and the protein	adapts E2 conformation	65
9196440054	transmembrane domain	ten a helices with a channel with two Ca2+ ions bound by 7 O2 atoms from glutamamte, aspartate, and threonine	66
9196451633	n domain	site of atp binding and hydrolysis	67
9196454390	p domain	accepts phosphate group from atp with an asp residue	68
9196458083	a domain	induces conformational change of t region releasing Ca2+	69