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| 11831792922 | Competitive inhibtors( reversible ) | Increase Km making the enzyme look like it has less affinity for substreate. And slows the reaction down but has the same VMax | 0 | |
| 11831792923 | Digitalis ((competitivee inhibitor) | Inhibts NA K+ pumps | 1 | |
| 11831792924 | Tetradotoxin (puffer fish) (competitive inhibitor) | Inhibits NA channels | 2 | |
| 11831792925 | Synthetic competitive inhibitor ( | Binds to homotropic site of enzyme | 3 | |
| 11831792926 | Noncompetitive inhibitor (reversible Inhibitiion) | Decrease Vmax because it wont allow. The enzyme to form a product. Km stays the. Same because it binds to the allosteric site because the inhibitor is a HETEROtropic inhibitor, not. Binding to the catalytic or homotropic site. | 4 | |
| 11831792927 | Caffine is? | Noncompetitive inhibitor (heterotropic)that binds to allotsteric site in phosodiesterase. Phosodiesterase normally breaks down cAMP. But this inhibitor allows cAMP to keep going. While this keeps going the more sugar and fat keeps being reeleased into the blood creating more energy. | 5 | |
| 11831792928 | Tomatoes | Noncompetive inhibitor (caffic acid)inhibits lipyogenase.. tomatoes are nattural anti inflammatory food source, slowing prostaglanden | 6 | |
| 11831792929 | Uncompetive inhibitor | Only binds to ES complex on allosteric site AFTER the enzyme has been bound. Tthis inhibitor prevents product formation. (Same with the others) DECREASE Vmax and DECREASE Km (making it seem like it has HIGHER affinity to the substrate). Pseudo Decrease in Km appears this way because, once uncompetitive inhibitor binds to ES Complex, it wont create product. This lack of creating products, will allow the other substrates to bind to free enzymes. Therefore making the enzymes seem like they have a HIGHER affinity. | 7 | |
| 11831792930 | Uncompetitve inhibitors in line weaver berk plot | Will have parallel lines to eachother because both vmax and km are different than normal. | 8 | |
| 11831792932 | Suicide inhibitors | 9 | ||
| 11837243844 | Nucleophile | A negatively charge molecule, which attacks the nucleus (attracted to the protons) (reactive species) (o-,s-,c-,N-) | 10 | |
| 11837243845 | Electrophile | Positively charged attracted to the electrons of the substrate (reactive species) (H+, C=O, C=NH+, O3-P=O | 11 | |
| 11837243846 | Nucelophiles and electrophiles will make? | Covalent bonds with another substrate, and creates the energy of the transition state to help make product formation | 12 | |
| 11837243847 | Covalent catalysis | Active site contains either a nucleophile or electrophile which creates a new transitional covalent bond with the intermediate. | 13 | |
| 11837243848 | Acid base catalysis | Active site is either a proton donor or a proton acceptor | 14 | |
| 11837243849 | Metal ion catalysis | A prosthetic group that has a negative or pos charge, that can create a nucleophile or electrophile attack. | 15 | |
| 11837243850 | Catalysis by approximation | Two substrates, bind them in the catalytic site and by induce fit moving them so close together they get a charge that induce product formation | 16 | |
| 11837243851 | Proteases (enzymes) | Are found almost everywhere, uses hydrolysis and breaks the chemical bond of water and chemical bond of peptide bonds C-N, and will places the OH group to the carbon, and the H+ to the Nitrogen. And the unpaired electrons go back to the carbon and nitrogen | 17 | |
| 11837243852 | Chymotrypsin | A serine protease enzymee | 18 | |
| 11837243853 | Chymotrypsin structure (Serine protease) has what components on the active site? | hydrophobic pocket- to attract trp, tyr, Phe, Met. This hydrophobic pocket when bound to the substrate aligns the protein, And basically allows catalysis of the protein to proceed. Bonds above a serine, which basically allows that serine to become a nucleophile (reactive species) to attack the coo- of the peptide bond. Oxyanion hole- has NH groups (amine) on glycine, near catalytic site to form stabilizing H bonds with the Coo- of the protein. Catalytic triad- in every catalytic site of serine proteases, you will find a aspartate, a histidine, and serine. They work together to do both acid base and covalent catalysis reaction | 19 | |
| 11837243854 | First step in catalytic traid? | To create stabilizing H bonds with ASP and NH group of histidine. The ASP neg charge is so strong that it pulls the hydrogen of NH group on histidine, which allows it to be a strong base. This pull also pulls ALL positive charges of histidine, all thats left is electrons of nitrogen. Since Histidine has lost it's electrons, the Nitrogen of histidine on the left side will take the electrons of Serine. |  | 20 |
| 11837244245 | 2nd step of chymotrypsin serine protease | This pull also pulls ALL positive charges of histidine, all thats left is electrons of nitrogen. Since Histidine has lost it's electrons, the Nitrogen of histidine on the left side will take the proton of Serine. This only happens in the catalytic site at this time, there is NO WATER which allows these strong bonds to happen. When the Proton from serine leaves it creates a ALKOXIDE ION = O- . The oxyanion hole stabilizes the O- of serine, so it doesnt form free radicals. |  | 21 |
| 11837244919 | 3. Step chymotrypsin serine protease | Serine is now a nucleophile because of the pull of the H bond from histidine. This serine will attack to partial postive charge of the C=O-. This creates a new covalent bond. This makes C have 5 covalent bond. |  | 22 |
| 11837245757 | Step 4 of chymotrpsin serine protease | Since Carbon covalent bond has 5 covalent bonds, this puts stress on the C, creating reactive species. The electrons will move to the oxygen of the C=O and creates a full negative charge on the OXYGEN. |  | 23 |
| 11837246037 | Step 5 of serine protease | Now carbon has 4 covalent bonds again, but once again the oxyanion hole, moves the electrons from the O- back onto the Carbon |  | 24 |
| 11837246640 | Step 6 of serine protease | Since the carbon ONCE AGAIN has 5 bonds, it will move the electrons over to the nitrogen on the amine group of the peptide bond. |  | 25 |
| 11837587330 | Step 6 continued of serine protease | Once the electrons are moved from carbon to nitrogen of the amine group. THIS TIME it actually breaks the amine group off. |  | 26 |
| 11837587630 | Step 8 of serine protease | Since half of the peptide is still there, and you have a Serine attached to the carbonyl group still, the enzyme has acylated" the serine oof the catalytic site R-C-R. It appears that the serine attached to the carbonyl group seem like its a suicide inhibitor. So now we need to break the acyl serine, to release the remainder of the substrate and we need to reset the enzyme. Since the serine is off the histidine H20 is able to be formed on to the histidine. Aspartate is still being a strong base. Now the histidine will take a H+ from water. |  | 27 |
| 11837587942 | Step 9 serine protease | The OH- from the breakage of water, goes on the carbonyl carbon. Which moves the electrons back onto the Oxygen creating O- once again. |  | 28 |
| 11837588385 | Step 10 serine protetase | The oxyanion hole AGAIN stabilizes the bonds by moving the electrons from the oxygen (O-) attached to the carbonyl carbon to the carbon. |  | 29 |
| 11837260377 | Step 7 of serine protease | The H that was stolen from serine on and went to histidine, go onto the Amide group leaving and becomes NH2+ |  | 30 |
| 11837586867 | Step 11 serine protease | The extra electrons on the carbonyl carbon will move onto the serine. Which breaks the Acyl bond R-C-R bond. The serine falls off. | 31 | |
| 11837586868 | Step 12 serine protease | Serine then goes back to the histidine thanks to the H+ that went on it from the water molecules. And the H+ will bond back to the O- on the serine. Resting the enzyme and allows it to work again. | 32 | |
| 11837586869 | Chymotrypsin and most serine proteases works best in what PH? | Alkaline ph less than 8 ph. The structure of chymotypsin works best in PH greater than 8 and others at PH of 7.4 physiological PH. This PH allows Histidine and aspartate to be a strong base. If the PH of the blood is low the histidine will be protonated not allowing the enzyme reaction to occur! | 33 | |
| 11837586870 | What would happen if water couldnt form in the catalytic site of serine protease? | Water allows the enzyme to reform, without water the Histidine would not be able to form back with the serine. The enzyme then could not be recycled. | 34 | |
| 11842279757 | Tyrpsin has what type of binding pocket? | A negative binding pocket that has aspartate in it. The aspartate pulls lysin and asparagine with + charged NH+ groups to the trypsin serine protease. | 35 | |
| 11842279758 | Elastase has what type of binding pocket? | Very narrow hydrophobic binding pocket, that restricts large hydrophobic molecules. Attracts glycine alanine and valine | 36 | |
| 11842279759 | Isozyme vs enzyme | Enzymes and isozymes can differ due to their amino acid structure. One example is tthe enzymes can have amide groups C-N) to the carbonyl carbon. While Esters (isozymes) can have ester groups attached to the carbonyl carbon (C-OR- | 37 | |
| 11842279760 | Actylcholenesterase | Enzyme at the neuro muscular junction and at neuron to neuron synapses, that breaks the neurotransmitter acetylcholine. Its a serine protease, still uses catalytic triad, it hydrolyzees a ester bond at acetylcholine instead of a peptide bond. SO it's a SERINE PROTEASE ISOZYME because it breaks down ester instead. | 38 | |
| 11842279761 | Cystein protease vs serine protease | Cystine protease replaces the. Serine group on the catalytic triad. Since cystine has the same resemlance as serine, only with a Sulfur instead..wworks the same as other proteases. | 39 | |
| 11842279762 | Aspartyl proteases vs serine protease | Aspartate catalyzes an acid base reaction that lead to covalent catalysis. Uses aspartate as the initiator . Does not resemble and appearance. Like. Serine. | 40 | |
| 11842279763 | Metaloproteases vs serine proteases | Uses a. Metal ion to attract a partial negitive charge to initiate catalyst | 41 | |
| 11842279764 | All proteases are similar due to the fact that? | They all use acid base catalysis and covalent catalysis strategies, they just initiate the peptide differently. | 42 | |
| 11842279765 | Metal. Ion catalysis | Metal ion catalysis uses a metal ion to then become a nucleophile. Or electrophile | 43 | |
| 11842279766 | Carbonic anhydrase is what type of catalysis? | Metal ion catalysis | 44 | |
| 11842279767 | Carbonic anhydrases. Use what to form bicarbonate ? | C02 and H20 | 45 | |
| 11842279768 | Carbonic anhydrase increase the rate of reaction bicarbonate by? | 5000 times faster. It is the fastest enzyme approaching the rate of diffusion | 46 | |
| 11842279850 | Carbonic anhydrase contains what type of. Prosthetic group? | Zinc ion bound with 3 coordinate covalent bonds with histidines, and 1 coordinate covalent bond with H20. A 4th histidine at the catalytic site serves as base to extract hydrogen from water, which gives the acid base portion. The hydrogen is then released into the solution. Then you form covalent catalysis with the carbon dioxide molecule. So the OH- is the nucleophile and C02 molecule combining is the covalent catalyst portion. The OH- C02 now bonded (HCO3-) forming bicarbonate, but is still attached to the 4th coordinate covalent bond of histidine. Water will then come in and break the bond from zinc releasing the bicarbonate. And this resets the enzyme. The histidine that took the proton from water, can add water back onto the zinc again froming the h20 coordinate covalent bond once again. |  | 47 |
| 11842279769 | Proteolysis | Regulates enzymes, enzymes that hydrolyze a peptide bond to allow the enzyme to be active again. | 48 | |
| 11842279770 | Zymogen is what? | An inactive enzyme precursor. Breaking part of. The zymogen will activate the enzyme, happens during a change in homeostasis. | 49 | |
| 11842279771 | Fibrinogen is what? | Is a ZYMOGEN (inactive precursor) that is used. To form clots when activated. Proteolysis is initiated by serine proteases thrombin. Thrombin binds to. Fibrinogen which breaks a part. Of fibrinogen and allows it to be activve to fibrin. | 50 | |
| 11842279772 | Monosaccharaides are | Are polyhydroxyls that have either a aldehyde group or a keytone group | 51 | |
| 11842279999 | Where is the carbonyl in both aldehyde and keytone placed in a structure? | Carbonyl is at the end of the carbohydrate structure which forms a aldehyde A keytone, the carbonyl is in the middle of the structure |  | 52 |
| 11842279773 | All monosaccharides have how many chiral carbons? | They have at least ONE Chiral carbon except DHA | 53 | |
| 11842280044 | Nomenclature of sugars |  | 54 | |
| 11842279774 | Chiral carbons allow for | Stereoisomers (non super imposable images of one another) | 55 | |
| 11842279775 | Most common sugars in nature are? | D-Glucose, D-fructose, D-ribose, D-galactose | 56 | |
| 11842279776 | Carbohydrate in bend light which way? | D- to the right , L- to the left | 57 | |
| 11842280118 | know how the structures are made for glucose, fructose, ribose, galatose |  | 58 | |
| 11842279777 | D-aldohexoses are generated when? | When the location of thee -OH group differs in either C2,C3,C4 | 59 | |
| 11842279778 | D glucose and d galactose are epimers because? | They only have one Carbon with hydroxl group difference. D glucose has its OH group on the right of chiral carbon 4 and D galactose has its OH group on the left at Chiral carbon #4 | 60 | |
| 11842279779 | Congenital lactose intolerance | Due to failure of galactose epimerase, since the body only recognizes glucose for energy and not galactose, the liver has an enzyme called galactose epimerase that changes the epimer galactose into glucose, failure of this results in lactose intolerance. | 61 | |
| 11842279780 | Glucose and mannose are epimers at which carbon? | Carbon #2 | 62 | |
| 11842279781 | Ketoses uses which suffix? | -Ulose (ribulose) EXCEPT: fructose, sorbose | 63 | |
| 11842279782 | Aldoses uses which suffix? | -ose (fructose is a ketose) | 64 | |
| 11842279783 | Fructose is found? | In fruits, its commonly broken down into glucose for energy | 65 | |
| 11842279784 | D-ribolose,D- xylulose | Pentuloses, for metabolism as well | 66 | |
| 11842279785 | URONIC acid | Is not a spontaneous reaction, O2 binds to the carbon at C6. This then forms a COOH carboxylic acid, which is a potential energy because COOH at 7.4 will creat a COO-, a Full negative charge will be place on the O. This O- can manipulate structures, to make them MORE water soluble. | 67 | |
| 11842279786 | aldonic acid | Is OXIDATION ON CARBON 1, NOT carbon 6. Which also can form a COOH carboylixic acid to form the ALDONIC acid (because aldose). This is used for carrier for drugs. remember COO- will make other groups water soluble | 68 | |
| 11842279787 | Monosachharides cyclic structures happens how? | In water aldohexoses or any monosaccharides potentially can have a nucleophile attack against itself. This is do to the presence of water, allow a hydroxyl (OH) group to have a negative charge do to the lone pair of electrons, that it took from water. This allows it to a be a nucleophile and can attack the 1st carbon, the carbonyl carbon. This attack breaks the C=O on the carbonyl and it forms a OH instead. The nucleophile OH group will lose its H+ and become only a O. It forms at the 5th carbon because its the most stable formation. NOTE* the nucleophile attack doesnt actually steal electrons, but the water encourages the nuucleophile attack | 69 | |
| 11842279788 | Hemiacetal and hemiketal | Is what the structure is called after a sugar 6 carbon, attacks itself (acetal if aldose) and ketal if ketone. | 70 | |
| 11842280179 | How many different structures of hemiacetal are there? | 2, Alpha and beta. Alpha looks like a fish and faces down to the fishes. Beta looks at the Birds. |  | 71 |
| 11842279789 | Anomeric carbon | Anomeric carbon is a non superimposable images, this is the nnew carbon. Its the only carbon bound by TWo electronegative Oxygen. All the other Carbons have only 1. Anomeric carbon in short is the new carbon in cyclic structure. Anomeric carbons have the strongest partial positive charge in the group | 72 | |
| 11842279790 | How many electrons are gained or loss with the hemiacytal is formed? | None, there are no loss or gain of electrons. | 73 | |
| 11842280313 | How is the hemiketal group formed? | In fructose, since it is a ketose. The OH group becomes the nucleophile in the 5th carbon OH group. But attacks the carbonyl group at C2. Anomeric carbon at C2. Its also a pentose |  | 74 |
| 11850757019 | Glycoside bond | Links two carbohydrates together, non spontaneous reaction(anabolic). Carbon 4 (nucleophile) of B-D glucose bonds to the anermeric carbon A-D glucose. The anomeric carbon has the highest partial postitive charge on the monnnosaccharide. Releasing H20... |  | 75 |
| 11850755685 | Which carbon hydroxyl group will become a nucleophile with disaccharides? | ANY hydroxyl group can become the nucleophile on the monosaccharides | 76 | |
| 11850756549 | Alpha 1-4 glycoside link | 1 carbon with 4 carbon on the beta d glucose | | 77 |
| 11852637595 | Reducing surgars | Are sugars that still have a free anomeric carbon available to be oxidized. It must be a carbon still bounded to two O molecules. |  | 78 |
| 11850755686 | Polysaccharides | Are sugar molcules that must have a free reducing sugar (free hydroxyl group) carbon so it can attack incoming saccharides. | 79 | |
| 11850755687 | Amylose | Is a alpha 1-4 glycosidic linkage of glucose, it makes a helical structure at 6 residues per turn (FOUND IN PLANTS) | 80 | |
| 11852665969 | Amylopectin | Is an alpha 1-4 glycosidic linkage, but at 24-30 residues it can have an alpha 1-6 glycossidic bond which causes branching and the branching allows my glucose molecules to bind, making it more complex. (Still in a helical structure) (FOUND IN PLANTS) glycogen is similar to amylopectin but 8-12 residues per turn. |  | 81 |
| 11850755688 | Why does glucose go into polymers of glycogen? | Because if glucose was in a monomer form only, the water would accumulate too much towards the molecules, and osmolarity would be our demise in the liver 5 mm of glucose would turn into 400mm of glucose if we didn't have glycogen | 82 | |
| 11850755689 | Cellulose uses which type of bonds? | B-D glucose bonds 1-4 instead of Alpha. And forms a linear structure. Cellulose is used for plants walls. And only organisms that can digest these are cows, and termites due to symbiosis with bacteria and parasites inside them to break the cellulose. | 83 | |
| 11850755690 | Chitin | Insect exoskeleton that contains B 1-4 glucose. A lot like cellulose but C2 has a bound acetylmine | 84 | |
| 11850755691 | Glucosamine | Are acetylamine groups on glucose | 85 | |
| 11850755692 | Peptidoglycan | Found also in CELL WALL, you get B.1-4 anyactyle glucosmine and anactyle nueronic acid on the glucose. Enzyme on SKIN and TEARS can break the peptidoglycan bonds, which in bacteria wont allow it to stay living. | 86 | |
| 11850755693 | Alagrose | Polysaccharides found in red algae and seaweed, that is used for drug capsules and biotechnology. | 87 | |
| 11850755694 | How are flavor receptors enhanced? | By PAMS (positive allosteric modulators) binding at the allosteric site to allow for further increase in the stimulation. Of our taste senses. | 88 | |
| 11850755695 | Glycosaminoglycans (sugar Protein sugar) (GAG) | Are used in the ECM, only found in ANIMALS and BACTERIA. They are able to form because of uronic acid, which oxidizes carbon 6. And glycosaminoglycans are used for glycocalyx proteins on membranes. The negitive charge due to Uronic acid, allow for a much large water retention and use for other protiens | 89 | |
| 11850755696 | Glycosaminoglycans (protein portion) | Uses the uronic acid side on carbon 6 oxidized to form covalent or. Non covalent linked to proteins or. Membranes. They can also create. Branches here. It also helps stabillize to stay onto the sugar. | 90 | |
| 11852665316 | Glycosaminoglycans structure (sugar side) | Are LARGE repetatiive structures rodlike HELICES. Has COO- and. Sulfate on opposite sides of the helix. (Remember when moleculs bindto. The hydroxyl groups they are glycosamines |  | 91 |
| 11850755697 | Aggrecans (other sugar side) | Similar. To linked. Protein which can bind covalently. Or. Non covalently to glucose. Polymer. But the aggrecan AGGREGATE. And form. Tthe other side of the sugar. Aggrecan. Core branches the glucose polymer off it | 92 | |
| 11850755698 | Bristle brush (glycosaminoglycans) | Created from the aggrecan core structure with the branches. Where you have a. Protein. Core as wire. Stick but the brissles. Are glycose polymers that have a FULL. Negative charge which supports the ECM. And also recruits proteins in signal transduction and communcation of the cell. | 93 | |
| 11850755699 | Hyaluronan (application) | Found in synovial fluid, has an EXTREME water retention and helps absorb and redistribute the water so it's less stressful compression (shock absorbers). Very important in bone articulation, bones will grind on eachother if this is impaired. | 94 | |
| 11850755700 | Hyluronase are what? | Enzymes in bacteria, that allows digestion of hyaluronan (GAGS) which does not allow the function of water retention and distribution properties.. This bacteria that causes this can be strepoccoccous, and staphlyoccous. | 95 | |
| 11850755701 | Types. Of GAGS that are important to know | hyruluenate has COO- in. It's structure only Chondroitin has COO- ANd SO4- making it more electronegative (tendons Keratin sulfate- has ONLY SO4- on C4 no uronic acid. | 96 | |
| 11850755702 | Heparan sulfate | Found and produced in all animal cells. Its sulfates SO4- varries in each heparan sulfate, but the SO4- is still used for protein interaction and bondage. | 97 | |
| 11850755703 | HerpARIN | HepARIN is a version of herpARAN but heparin uses more sulfates. Is produced by mast cells. It binds ot antithrombrin, and thrombrin both to create a bridge, when antithrombrin binds with thrombrin to prevent blood clots. SO basically Heparin is a version of heparan that has a strong NEGATIVE pull that pulls positive thrombrin and antithrombrin to bind together. | 98 | |
| 11865046861 | Proteoglycan | A macromolecule with one or more glycosaminoglycans covalently bound to membrane proteins or secreted proteins. Basically the bristle brushes attached to the membrane proteins | 99 | |
| 11865046862 | Glycoprotein is bbigger or smaller than proteoglycan? | Much smaller its an oligosaccharide bound to intracellular or extracelluar protein but both glycoproteins and proteoglycans form the glycocalyx. | 100 | |
| 11865046863 | Proteoglycan and gllycoproteins both help in: | -Protein binding -Recruiting hormones and ligands to receptors -concentrate a ligand at the cell surface - hold association of protein such as collogen for tensile strenght | 101 | |
| 11865046864 | 2 ways carbs bind to proteins: | 1. O-linked- oxygen becomes a nucleophile and pulls the SER or THR to itself, 2. N-linked- ASP is the nucleophile and pulls the anomeric carbon. | 102 |
