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| 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 |
