Term
| What type of protein arrangement are most enzymes? (primary, secondary, tertiary, quaternary) |
|
Definition
| Tertiary, thus globular proteins |
|
|
Term
| How often do enzymes for side products? |
|
Definition
| Rarely, since they are highly regulated |
|
|
Term
| What is the inactive form of an enzyme called? (2 names meaning the same thing) |
|
Definition
|
|
Term
| How in an inactive enzyme made active? |
|
Definition
| Be an irreversible cleabage of one or more peptide bonds |
|
|
Term
| The proenzyme is chymotrypsinogen, so what is the active form called? |
|
Definition
|
|
Term
| What term refers to an enzyme without a cofactor? |
|
Definition
|
|
Term
| What term refers to an enzyme with a bound cofactor? |
|
Definition
|
|
Term
| What term refers to any non-protein molecule which aids the function of an enzyme? |
|
Definition
|
|
Term
| What can be said about the bond between an enzyme and its cofactor? |
|
Definition
| May be loosely or tightly bound to the enzyme |
|
|
Term
| What type of charge do cofactors provide to enzymes? How does this help? |
|
Definition
| Cofactors provide a high concentration of positive charge which aids in the binding os small molecules to enzymes |
|
|
Term
| Do cofactors help or inhibit redox reactions? |
|
Definition
|
|
Term
| Do cofactors help or inhibit catalysis? |
|
Definition
|
|
Term
| What does a cofactor do to an enzyme substrate? |
|
Definition
|
|
Term
| What does a cofactor do to an enzyme substrate in regards to the active site? |
|
Definition
| The cofactor helps orient the substrate in the active site |
|
|
Term
| What type of ions would be considered activators in regards to cofactors for enzymes? |
|
Definition
| Inorganic ions such ad Mg++, Mn++, and Ca++ |
|
|
Term
| What type of ions would be considered metalloenzymes in regards to cofactors for enzymes? What is the bond strength? |
|
Definition
| Tightly held metal ions such as Zn++, Se+, and K+ |
|
|
Term
| What type of group could be described as a tightly bound pigment molecule, such as biotin? |
|
Definition
|
|
Term
| Where are most coenzymes derived from? |
|
Definition
| Vitamins, in particular the B vitamins Niacin (Nicotinic acid) and Riboflavin |
|
|
Term
| What is the name of coenzymes in redox reactions? |
|
Definition
| Oxido-reductases such as hydrogenases |
|
|
Term
| During the NAD+ Coenzyme redox reaction, what are the 2 cosubstrates? What is the function? |
|
Definition
| NAD and NADP Which accept and donate hydrogens in dehydrogenase reactions |
|
|
Term
| During the NAD+ coenzyme redox reaction, what molecule accepts a hydride ion? What is the end result? |
|
Definition
| NAD+, which reduces it to NADH |
|
|
Term
| What helps the oxidation of lactate to pyruvate? |
|
Definition
|
|
Term
| Describe the oxidation of lactate to pyruvate? |
|
Definition
| lactate loses 2 electrons as hydride ions. Thus, a proton is release. |
|
|
Term
| What type of bond occurs between an enzyme and substrate and why? |
|
Definition
| Noncovalent because if it were covalent, the substrate would not be able to be released |
|
|
Term
| What is the formulaic reaction of an enzyme? ( X+X .....) |
|
Definition
| Enzyme + Substrate <--->(notice rxn arrow) Enzyme-Substate(notice the bond) ---->(notice rxn arrow) Enzyme + Product |
|
|
Term
| How could one describe the rigidity of an enzyme? |
|
Definition
|
|
Term
| What can be said about the shape of an enzyme-substrate during the transition stage? |
|
Definition
| Both enzyme and substrate change conformation in the transition state |
|
|
Term
| What is the current theory of enzyme binding? |
|
Definition
|
|
Term
| What is the difference between non-competitive inhibition and un-competitive inhibition? |
|
Definition
In non-competitive inhibition, the inhibitor binds to the enzyme which prevents the substrate from forming a bond to the enzyme.
In uncompetitive inhibition, the substrate and enzyme form a bond. However, the inhibitor binds to this complex which ultimately prevents the product from forming. |
|
|
Term
| What is an irreversible inhibitor? Where does this take place on the enzyme. |
|
Definition
| A covalent bond forms between the inhibitior and the enzyme. This occurs at a side chain on the active site of the enzyme. |
|
|
Term
| How could one combat a non-competitive inhibition? |
|
Definition
|
|
Term
| Where does the inhibitor bind do during non-competive inhibition? What about competitive inhibition? |
|
Definition
Noncompetitive- inhibitior binds to allosteric site
Competitive- inhibitior binds to active site, thus the inhibitor must have a very similar structure to the substrate. |
|
|
Term
| Where would one likely observe uncompetitive inhibition? |
|
Definition
| In a reaction where enzymes bind more than one substrate. |
|
|
Term
| In uncompetitive inhibition, where does the inhibitor bind. |
|
Definition
| It binds to the allosteric site after the substrate binds to the enzyme. Thus, preventing the product from forming. |
|
|
Term
| What is an example of irreversible inhibiton? |
|
Definition
| A sulfhydryl group binding to an enzyme. |
|
|
Term
| What is the unit for measurement of an enzyme? How is it reported in the lab? |
|
Definition
Amt. product per liter per second
Reported in the lab as units per liter |
|
|
Term
| If conc. S is low what order of kinetics is observed? How could one describe the rate of reaction? |
|
Definition
| First order so the ror is proportional to the substrate conc. |
|
|
Term
| Is conc. S is high, what order of reaction is observed? |
|
Definition
|
|
Term
| With zeroth order, what is being measured? |
|
Definition
| Enzyme capability, not the substrate |
|
|
Term
| Which order of reaction has a constant rate? Why? |
|
Definition
| Zeroth order because of substrate saturation |
|
|
Term
| What does Km stand for in michelis-menten? |
|
Definition
| Conc. S at vmax divided by 2 |
|
|
Term
|
Definition
| The affinity of the enzyme relative to the substrate |
|
|
Term
| How is Km used in a clinical setting? |
|
Definition
| Shows what conc. S is needed for an enzyme measurement |
|
|
Term
| What is the michaelis-menten equation? |
|
Definition
|
|
Term
| What does the turnover number mean? |
|
Definition
| The amount of product formed Ina unit of time with saturated enzyme |
|
|
Term
| What does the rate constant refer to in a catalytic enzyme? |
|
Definition
| Number of catalytic cycles and enzymeS active site undergoes per unit of time |
|
|
Term
| What are the graphical differences between michaelis menten and linweaver burke? |
|
Definition
Mm - parabola
Lb- y=mx+b plot |
|
|
Term
| What two ways can an Allosteric site act as an activator? |
|
Definition
| Stimulate binding of substrate or release of product |
|
|
Term
| What protein strucutre is an enzyme with an Allosteric region? |
|
Definition
|
|
Term
| How do Allosteric enzymes follows michaelis menten? |
|
Definition
|
|
Term
| How are Allosteric enzymes regulated. |
|
Definition
| Pathway substrates or products |
|
|
Term
| What is significant about an enzyme having a high concentration in plasma? |
|
Definition
| Disease must be present and cell must be disrupted |
|
|
Term
| Where are enzymes most likely found in respect to cellular location? |
|
Definition
|
|
Term
| What Types of carbohydrates do d and l forms exist? |
|
Definition
|
|
Term
| What types of environment can glucose change conformation? |
|
Definition
| Aqueous environment of the body |
|
|
Term
| Which sugars are always reducing agents? |
|
Definition
|
|
Term
| How can a disaccharide become a reducing sugar? |
|
Definition
| If there's a carbonyl group after the glycosidic bond |
|
|
Term
| How is glucose related to the brain, rbc's, and the eye? |
|
Definition
| It is the only source of energy |
|
|
Term
| What are the structural elements of glucose found in the body? |
|
Definition
|
|
Term
| What sugar is used as an artificial sweetener? |
|
Definition
|
|
Term
| What sugar is necessary for the synthesis of lactose, Glycolipids, phospholipids,etc? |
|
Definition
|
|
Term
| What two sugars form lactose? |
|
Definition
|
|
Term
| What is the physiology of lactase deficiency? |
|
Definition
| Inability to hydrolysis lactose bond |
|
|
Term
| What is the product of two glucoses bound together? |
|
Definition
|
|
Term
| What is the breakdown product of starch? |
|
Definition
|
|
Term
| What nonreducing sugar is formed by glucose and fructose? |
|
Definition
|
|
Term
| After a glycosidic bond forms, what significant bond event occurs? |
|
Definition
|
|
Term
| What is the breakdown product of cellulose? |
|
Definition
|
|
Term
| What is the difference between cellubiose and maltose? |
|
Definition
| Glycosidic linkage site is different even though both are the products of 2 glucose molecules |
|
|
Term
| Where is one likely to find oligosaccharides? What are oligosaccharides |
|
Definition
| Glycoproteins and glycolipids. Oligosaccharides are small Polymers |
|
|
Term
| What are the 4 homopolysaccharides? |
|
Definition
| Starch, glycogen, cellulose, chitin |
|
|
Term
| What is amylose and how is it formed? |
|
Definition
| Long unbranched chain of d-glucose linked by multiple 1,4glycosidic bonds |
|
|
Term
| What is amylopectin and how is it formed? |
|
Definition
| Branched glucose polymer linked by 1,4 and 1,6 glycosidic bonds |
|
|
Term
| What are glycosaminoglycans derived from. |
|
Definition
| Mostly amino acids and linear disaccharides |
|
|
Term
| What provides joint fluidity and water retention in joints? |
|
Definition
|
|
Term
| How are peptide glycine held together? |
|
Definition
|
|
Term
| What is the minimum for a parallel peptide chain? |
|
Definition
|
|
Term
| What are proteoglycans, where are they found, and what is their function? |
|
Definition
| Protein an sigh carbohydrate content, found in extrecellular matrix, aids in support and elasticity |
|
|
Term
| What is a glycoconjugate? |
|
Definition
| Carbohydrate and another molecule bound together |
|
|
Term
| What are the three groups of glycoconjugates? |
|
Definition
| Proteoglycans Glycoproteins glycolipids |
|
|
Term
| How are glycoproteins linked together? (molecules) |
|
Definition
| By the nitrogen and oxygen |
|
|
Term
| Where can glycoproteins be found? |
|
Definition
| Cells, membranes, and Ecf |
|
|
Term
| What is the purpose of transferrin? |
|
Definition
|
|
Term
|
Definition
| Breakdown of glycogen to glucose |
|
|
Term
|
Definition
| Synthesis of glycogen from glucose |
|
|
Term
|
Definition
| Use of glucose by the body |
|
|
Term
| Describe embden Meyerhof pathway. |
|
Definition
| Glucose enters cell, glucose phosphorylated, glucose to fructose, fructose phosphorylated, 2 three carbon molecules are formed, 1,3 biphosphoglycerate is formed, A phosphate is removed to form ATP, Pyruvate to lactate |
|
|
Term
| What are the net products of anaerobic glycolysis? |
|
Definition
| Net 2 ATP, 2 nadh, 2 pyruvate |
|
|
Term
| How is glucose converted to glucose-6-phosphate? |
|
Definition
| By energy investment and glucokinase |
|
|
Term
| How does glucose six phosphate become fructose six phosphate? |
|
Definition
| PhosphoHexose and isomerase |
|
|
Term
| How does fructose six phosphate become fructose 1,6 biphosphate? |
|
Definition
| ATP investment and Phosphofructokinase |
|
|
Term
| What molecule is split into 3 carbon molecules during anaerobic glycolysis? What are the 3 carbon molecules? |
|
Definition
Fructose 1,6 biphosphate.
Forms glycerAldehyde 3 phosphate and Dihydroxyacetone phosphate |
|
|
Term
| How is glyceraldehyde 3 phosphate converted to 1,3 biphosphoglycerate? |
|
Definition
| By forming an nadh and by Glyceraldehyde 3 Phosphate dehydrogenase |
|
|
Term
| How does 1,3 biphosphoglycerate become its product and what is it? |
|
Definition
| An ATP is phosphorylated forming 3- phosphoglycerate by way of phosphoglycerate kinase |
|
|
Term
| How does 3-phosphoglycerate become its product and what is it? |
|
Definition
| 2-phosphoglycerate by way of phosphomutase |
|
|
Term
| How does 2-phosphoglycerate become its product and what is it? |
|
Definition
| Phosphoenolpyruvate is formed by way of enolate |
|
|
Term
| How does phosphoenolpyrivate become pyruvate? |
|
Definition
| Pyruvate is formed by adp phosphorylating into ATP by way of pyruvate kinase |
|
|
Term
| What does enolase do to 2-phosphoglycerate to turn it into PEP? |
|
Definition
| It oxidizes it by removing a hydrogen |
|
|
Term
| How is pyruvate converted to lactate |
|
Definition
| In the presence of lactate dehydrogenase and nadh |
|
|
Term
| Which cells could one find lactate dehydrogenase? Which organ ses LD during gluconeogenesis? |
|
Definition
|
|
Term
| How is hexokinase activity regulated |
|
Definition
| By glucose-6-phosphate activity |
|
|
Term
| What controls phosphofructokinase? |
|
Definition
| Concentration of fructose1,6-phosphate and fructose 6 phosphate |
|
|
Term
| How is pyruvate kinase activated |
|
Definition
| By the forward reaction of fructose 1,6 phosphate |
|
|
Term
| In the pentode phosphate shunt how is the main product generated and what is it? |
|
Definition
| Nadh generated from oxidoreductase enzymes reacting with nadp |
|
|
Term
| What is the purpose of nadh in red blood cells? |
|
Definition
| It reduces cysteine containing gsh molecules |
|
|
Term
| What exactly is gsh and what is its purpose? |
|
Definition
| Coenzyme with glutathione reductive. It prevents the oxidation of sulfhydryl groups into disulfide bonds |
|
|
Term
| How does the pentose shunt protect a red blood cell |
|
Definition
| It reduces oxidative damage |
|
|
Term
| What are the pentoses used for that were created in the pentose shunt? |
|
Definition
| Used to help build nucleotides |
|
|
Term
| What is the initiating molecule in the 2,3 BPG pathway? |
|
Definition
|
|
Term
| What is the purpose of 2,3 BPG? |
|
Definition
| It is the negative controller in Oxygen affinity for hemoglobin a. It also reduces the amount of ATP production |
|
|
Term
| What intermediate is galactose converted into? |
|
Definition
|
|
Term
| What 3 general structures are galactose molecules used in the synthesis of? |
|
Definition
| Glycolipids, proteoglycans, glycoproteins |
|
|
Term
| What two enzymes are ATP producing in the embden meyerhof pathway? |
|
Definition
|
|
Term
| What does a g6pd deficiency cause? Why is g6pd important |
|
Definition
| Hemolytic anemia. Helps control proper cell growth because it is required to make nadh in red blood cells |
|
|
Term
| Why is the hmp pathway so important 2 reasons? |
|
Definition
| It links multiple pathways together Such as allowing carbohydrates into the Glycolytic pathways and also aids in the production of nadph from nadp |
|
|
Term
| What is the role of pyruvate kinase? |
|
Definition
| Regulator enzyme for gluconeogenesis |
|
|
Term
| What are ros' and what do they do? |
|
Definition
| They are reactive oxygen species and cause oxidative stress. Antioxidants are fighting these |
|
|
Term
| Is gluconeogenesis anabolic or catabolic? |
|
Definition
|
|
Term
| How is gluconeogenesis initiated? |
|
Definition
| What blood glucose levels reach the lower end during a fasting state |
|
|
Term
| What is the starting molecule of gluconeogenesis? |
|
Definition
|
|
Term
| Where are the products of gluconeogenesis created? Why? |
|
Definition
| Liver and kidney cells because they contain glucose-6-phosphate |
|
|
Term
| What two things can the body do with g6p? |
|
Definition
| Store it as glycogen or transport it to the liver to be converted to glucose |
|
|
Term
| How is pyruvate converted to oxaloacetate? |
|
Definition
|
|
Term
| Pur carboxylase + pyr = ? |
|
Definition
|
|
Term
| Where does the pyruvate come from in gluconeogenesis? |
|
Definition
| Lactic acid or deamination of alanine |
|
|
Term
| What is pyruvate converted into during gluconeogenesis? What occurs next? |
|
Definition
| PEP which is then converted into 2 phosphoglycerate which mutates into 3 phosphoglycerate |
|
|
Term
| What happens to 3 phosphoglycerate in gluconeogenesis? |
|
Definition
| 3 phosphoglycerate is converted into 1,3- diphosphoglycerate |
|
|
Term
| Gluconeogenesis: 1,3 dog ---> ? |
|
Definition
| Glyceraldehyde 3 phosphate |
|
|
Term
| How is fructose 1,6 phosphate formed during gluconeogenesis? |
|
Definition
| By the combination of glyceraldehyde 3 phosphate and dihydroxyacetone |
|
|
Term
| Gluconeogenesis: what are the steps for converting Frucotse 1,6 phosphate into glucose? |
|
Definition
| Fructose 1,6phosphate -> fructose 6 phosphate --> glucose 6 phosphate -> glucose |
|
|
Term
| What part of the cell does gluconeogenesis end ? |
|
Definition
|
|
Term
| In liver cells where does the conversion of g6p to glucose actually occur and where is it release afterwards? |
|
Definition
| Converted in smooth er and release into the cytoplasm |
|
|
Term
| What 2 hormones regulate gluconeogenesis? |
|
Definition
|
|
Term
| I. Gluconeogenesis what does acetyl coa activate and deactivate? |
|
Definition
| Activates pyruvate Carboxylase while inhibiting pyruvate Dehydrogenase |
|
|
Term
| What is the process for maintaining homeostasis throughout the body? |
|
Definition
|
|
Term
| What two places is glycogen stored and what is the physiology of eachlaces storage. |
|
Definition
Liver cell- maintains homeostasis throughout body
Muscle cell- provides glucose to muscles when in need |
|
|
Term
| What is the starting material for glycogenesis? |
|
Definition
|
|
Term
| Describe the basic steps of glycogenesis? |
|
Definition
| G6p converts to g1p which then converts to Uridine diphosphoglucose. UDP then binds to other glycogen by a 1,4 linkage in the presence of glycogen synthase. |
|
|
Term
| How are glucose transporter 2 and gluconeogenesis kinase activated? |
|
Definition
| By high levels of glucose in the blood |
|
|
Term
| During glycogenesis, where does extra glucose 6 phosphate go? |
|
Definition
| Goes into glycolysis or gets turned into triglycerides |
|
|
Term
| How does glycogen synthase become activated? |
|
Definition
| It's is phosphorylated by protein kinase |
|
|
Term
| During glycogenesis how is protein kinase activated? |
|
Definition
|
|
Term
| With glycogen synthetase, how are 1,6 glycosidic bonds formed? |
|
Definition
|
|
Term
| How is stored glycogen made available to the body? |
|
Definition
|
|
Term
| What 3 things stimulate glycogenolysis? |
|
Definition
| High cAMP, glucagon, and epinephrine |
|
|
Term
| What type of bond breakage occurs with glycogenolysis? |
|
Definition
|
|
Term
| What effectively slows down glycogenolysis? |
|
Definition
|
|
Term
| How is glycogen converted to glucose1phosphate during glycogenolysis? |
|
Definition
| Glycogen phosphorylase by breaking 1,4 linkages |
|
|
Term
| What is the purpose of Debranching enzyme transferase in glycogenolysis? |
|
Definition
| It breaks trisaccharides from the already broken branch and then reattached the trisaccharides to the terminal end of the starting glycogen molecule |
|
|
Term
| After Debranching enzyme transferase performs its activities, how can glucose be obtained from the chain? |
|
Definition
| 1,6 glucosidase hydrolyses one glucose from the existing branch. |
|
|
Term
| Where is glucagon produced? |
|
Definition
|
|
Term
| Describe the glucagon process. |
|
Definition
| Glucagon binds to a receptor which releases g proteins. These then stimulate FTP production. G proteins then break and dissociate 1 unit binding to Adenyl cyclase which then converts ATP into cAMP. cAMP then binds to protein kinase |
|
|
Term
| When cAMP binds protein kinase, what 2 activities occur? |
|
Definition
Activates inhibitors To phosphoprotein phosphatase
Works with ATP to provide Pi for converting glucose into glucose1phosphate |
|
|
Term
| What is pyruvate carboxylated into to start gluconeogenesis? |
|
Definition
|
|
Term
| What must happen to OAA to start glycogenolysis? |
|
Definition
| Carboxylase group and a phosphate must be added in order to form PEP |
|
|
Term
| What process is activated by the addition of two phosphate groups to gmp? |
|
Definition
|
|
