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211 Cards in this Set
- Front
- Back
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The activity of which enzyme controls the rate of glycolysis?
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Phosphofructokinase
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A glycolytic enzyme that catalyzes the irreversible transfer of a phosphate from ATP to fructose-6-phosphate.
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Phosphofructokinase
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What are the reagents and products in a reaction with phosphofructokinase?
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fructose-6-phosphate + ATP ---- fructose-1,6-bisphosphate + ADP
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What enzyme is stimulated by ADP and AMP and is inhibited by ATP and Citrate?
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Allosteric enzyme
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What is an important allosteric activator of the allosteric enzyme, and an allosteric inhibitor of _____?
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Fructose-2-6-biphosphate
Fructose-1-6-biphosphate |
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What enzyme converts fructose-1-6-bisphosphate into two 3-carbon metabolites, _____ _____ and _____?
What is this reaction called? |
Aldolase
dihydroxyacetone phosphate glyceraldehyde-3-phosphate Aldolytic reaction of glycolysis |
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Where is aldolase plentiful anatomically?
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Skeletal and heart muscle tissues
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Glycolysis occurs in the cytoplasm in the _____ of oxygen.
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Absence
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How many molecules of ATP are used to phosphorylate glucose and start glycolysis?
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2
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Two molecules of _____ capture H+ and are reduced to 2 molecules of _____ in glycolysis.
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NAD+
NADH+H+ |
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How many molecules of ATP are produced by substrate phosphorylation?
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4
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What is the end product of glycolysis?
What can this undergo? |
Pyruvate
Either aerobic respiration in mitochondria or anaerobic respiration (fermentation) |
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What is the net gain of ATP in glycolysis?
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2
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What catalyzes the isomerization of glucose-6-phosphate to fructose-6-phosphate?
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Phosphoglucose isomerase
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What interconverts dihydroxyacetone phosphate and glyceraldehyde-3-phosphate?
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Triose phosphate isomerase
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The first sign of myocardial infarction in a patient is a high plasma level of which enzyme?
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Creatine Kinase (CK)
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In liver disease which two enzymes will be elevated in the plasma?
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Glutamate-oxaloacetate transaminase (GOT)
Glutamate-pyruvate transaminase (GPT) |
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What enzyme functions in the transamination of alpha-ketoglutarate and L-alanine to glutamate and pyruvate?
What is another name for this? |
Glutamate-pyruvate transaminase (GPT)
Alanine aminotransferase (ALT) |
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What is another name for Glutamate-oxaloacetate transaminase (GOT)
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Aspartate aminotransferase (AST)
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What are the enzymes most seen in the heart?
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Creatine Kinase
Lactate dehydrogenase Glutamate-oxaloacetate transaminase Glutamate-pyruvate transaminase |
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What amino acids are not transaminated?
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Lysine
Serine Threonine |
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What is the first step of amino acid catabolism?
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Removal of alpha-amino group
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How is nitrogen transferred from one amino acid to another?
What is involved? |
Transamination reactions
2 different pairs of amino acids & corresponding alpha-keto acids |
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What usually serves as one of the two pairs that are utilized in amino acid transaminase reactions?
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Glutamate
alpha-ketoglutarate |
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What is required for transaminases to catalyze the transfer of amino acids?
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Pyridoxal phosphate
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What reactions result in the liberation of an amino group as a free ammonia (NH3)
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Oxidative deamination reaction
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Where do oxidative deamination reactions generally take place?
What are the products? |
Liver and Kidney
alpha-ketoacids (energy) and ammonia (source of N in urea synthesis) |
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What enzyme is used on Glutamate in a deamination reaction?
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Glutamate dehydrogenase
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What enzyme is used on Histidine in a deamination reaction?
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Histidase
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What enzyme is used on Serine and threonine in a deamination reaction?
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Serine dehydrogenase
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What kind of reaction shares a common prosthetic group?
What is that group? |
Aminotransferases (transaminases)
Pyridoxal phosphate (PLP) |
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Pyridoxal phosphate (PLP) is the coenzyme form of what?
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Pyridoxine or vitamin B6
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What functions as an intermediate carrier of amino groups at the active sites of aminotransferases?
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PLP or Pyridoxal phosphate
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PLP undergoes reversible transformations between its aldehyde form, _____ _____, which can accept an amino group, and its aminated form, _____ _____, which can donate its amino acid to an alpha-keto acid.
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Pyridoxal phosphate (PLP)
Pyridoxamine phosphate (PMP) |
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Oxidative deamination occurs primarily on _____ _____ because it was the end product of many transamination reactions.
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Glutamic Acid
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What is an enzyme that catalyzes the oxidative deamination of glutamate?
What is released from this reaction? What is formed? What class does this enzyme belong to? |
Glutamate dehydrogenase
Ammonia alpha-ketoglutarate Oxidoreductase class |
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Glutamate dehydrogenase is unusual in that it can either use _____ or _____ as a coenzyme.
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NAD
NADP |
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Both asparate aminotransferase (AST) and alanine aminotransferase (ALT) are _____.
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Transaminases
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_____ deaminates glutamine to glutamate and an ammonium ion
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Glutaminase
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_____ deaminates asparagine to aspartate and ammonium ion.
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Asparaginase
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_____ is deaminated by histidase to form ammonium ion (NH4+) and _____.
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Histidine
Urocanate |
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What is serine converted to by serine dehydratase?
Threonine? |
Pyruvate
alpha-ketobutyrate |
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Carbonic anhydrases are _____-containing enzymes that catalyze the reversible reaction between carbon dioxide hydration and bicarbonate dehydration.
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Zinc
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What does Carbon dioxide exist in equilibrium with in the body?
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Bicrabonate HCO3-
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What can be freely diffused in and out of the cell?
Bicarbonate/Carbon dioxide? |
Carbon Dioxide
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What is the reaction that carbonic anhydrase catalyzes?
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H2O + CO2 <---> H+ + HCO3-
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What is one of the fastest known enzymes?
Where is this enzyme found? |
Carbonic Anhydrase
Concentration in Erythrocytes |
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Within the erythrocyte what does carbonic anhydrase facilitate?
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Combination of carbon dioxide and water to form carbonic acid
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Carbonic Anhydrase also functions in the _____ with the reabsorption of bicarbonate ion.
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Kidney
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How is most CO2 transported in the blood?
What part of the blood is its conversion more rapid in? Why? |
Bicarbonate ion (HCO3-)
Whole blood more than plasma Whole blood contains erythrocytes |
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What part of the electron transport chain accepts only electrons?
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Cytochrome b
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Named for the fact that electrons are transported to meet up with oxygen from respiration at the end of the chain.
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Electron transport (respiratory) chain
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Where is the electron transport chain located?
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Inner mitochondrial membrane
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_____ _____ and _____ _____ by oxidative phosphorylation proceed continuously in all cells of the body that contain mitochondria.
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Electron transport
ATP Synthesis |
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What are the components of the electron transport chain?
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FMN
Coenzyme Q Cytochromes (b,c,a,a3) Oxygen |
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Part of the electron transport chain that receives electrons from NADH and transfers them through _____ centers to coenzyme Q.
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FMN
Fe-S |
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What is FMN derived from?
What is NAD derived from? |
Riboflavin
Niacin |
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What part of the electron transport chain receives electrons from FMN and also through Fe-S centers from _____?
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Coenzyme Q
FADH2 |
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How is coenzyme Q derived?
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Body synthesizes it
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What part of the electron transport chain receives electrons from the reduced form of coenzyme Q?
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Cytochromes (b,c,a,a3)
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What does each cytochrome consist of?
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Heme group associated with a protein
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What is Cytochrome a+a3 called?
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Cytochrome oxidase
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What is heme synthesized from in humans?
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Glycine and succinyl CoA
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What ultimately receives electrons at the end of the electron transport chain and is then reduced to water?
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Oxygen
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What is a nonprotein substance (organic cofactor) that combines with an apoenzyme to form a haloenzyme?
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Coenzyme
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What is the protein portion of a complex enzyme?
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Apoenzyme
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What is a complete catalytically active enzyme?
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Haloenzyme
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Enzymes are _____. Most are large _____.
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Enzymes
Proteins |
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How does an enzyme speed up a reaction by binding to a reagent in the reaction?
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Speeds up activation energy
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What determines the function of an enzyme?
Enzymes are _____ specific. |
Shape
substrate |
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The arrangement of molecules on an enzyme produces an area known as the _____ _____ within the specific substrates will fit.
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Active Site
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What classification catalyzes a redox reaction?
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Oxidoreductases
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What classification transfers a functional group reaction?
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Transferases
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What classification causes hydrolysis reaction?
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Hydrolases
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What classification break C-O, C-C, or C-N bonds?
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Lyases
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What classification Arranges functional groups?
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Isomerases
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What classification joins two molecules -- for example, DNA ligase joins pieces of DNA?
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Ligases
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What effects the activity of an enzyme?
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Substrate concentration
pH Temp. Enzyme concentration |
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The enzymatic model that assumes that enzymes have flexible conformations is called _____ _____.
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Induced fit
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What is the active precursor of an enzyme?
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Proenzyme
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What enzyme is used to dissolve blood clots?
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Plasmin or fibrinolysis
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Plasmin is normally present in the blood in its inactive form called _____.
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Plasminogen
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What is a soluble protein normally present in the plasma that is essential to the blood clotting process?
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Fibrinogen
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What is fibrinogen converted to?
By What? Soluble or Insoluble? |
Fibrin
Thrombin Insoluble |
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What is the protein precursor of Thrombin?
Where is this formed? |
Prothrombin
Liver |
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What specifics are required to converted prothrombin to thrombin?
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Thromboplastin
Calcium Ions |
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What linkages does Thrombin act on in fibrinogen to produce Fibrin?
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Arginyl-glycinr linkages
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A zymogen is converted to the active enzyme form in which way?
Where is this done? |
Removal of a peptide fragment
Lumen of the digestive tract |
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What are enzymatically inactive precursors of proteolytic enzymes?
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Zymogens
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The _____ enzymes that hydrolyze proteins are produced and secreted as zymogens in the _____ and _____.
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Digestive
Stomach Pancreas |
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What mediates the release and activation of the pancreatic zymogens?
|
Cholecystokinin
Secretin |
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Where is Pepsinogen synthesized?
What is the active form? |
Stomach
Pepsin |
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Where is chymotrypinogen synthesized?
What is its active form? |
Pancreas
Chymotrypsin |
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Where is Procarboxypeptidase A synthesized?
What is its active form? |
Pancreas
Carboxypeptidase A |
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Where is Trypinogen synthesized?
What is its active form? |
Pancreas
Trypsin |
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Where is Procarboxypeptidase B synthesized?
What is its active form? |
Pancreas
Carboxypeptidase B |
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Where is Proelastase synthesized?
What is its active form? |
Pancreas
Elastase |
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What are starch molecules broken down by?
What is another name for this? |
Amylase
Ptyalin |
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Amylase is the name given to _____ _____ enzymes that break down starch into glucose molecules.
|
Glycoside hydrolase
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What are the three classifications of amylases?
|
alpha
beta gamma |
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By acting in random locations what form of amylase breaks down long-chain carbohydrates.
|
Alpha-amylase
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What does alpha-amylase break down? Into What?
|
Amylose - maltotriose and maltose
Amylopectin - amylose, maltose, limit dextran |
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What is faster?
alpha or beta amylase Why? |
alpha
Can act anywhere on the substrate |
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What are typically alpha-amylases in the body?
|
Salivary and pancreatic amylases
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What form of amylase works from the non-reducing end, and catalyzes the hydrolysis of the second alpha-1,4 glycosidic bond, cleaving off two glucose units at a time?
|
Beta
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What form of amylase cleaves the last alpha-1,4-glycosidic linkages at the non-reducing end of amylose and amylopectin, yielding _____, and will also cleave alpha-_____-glycosidic linkages?
|
gamma
glucose 1,6 |
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What are various branched polysaccharides fragments that remain following the hydrolysis of starch?
|
Limit dextrins
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Where are dissaccharides and small glucose polymers hydrolyzed?
By what? |
Brush boarder of intestine
lactase, sucrase, maltase, alpha-dextrinase |
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Only _____ are absorbed in the small intestine.
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Monosaccharides
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What does lactase degrade lactose into?
|
Glucose and galactose
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what cleaves a glucose linked 1,6 to another glucose as is found at the branch points in starch and glycogen?
|
Isomaltase
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What does sucrase degrade sucrose into?
|
Glucose and fructose
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If a patient has von Gierke's disease they are missing the enzyme _____, which converts _____.
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Glucose-6-phosphate
glucose-6-phosphate to glucose |
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G6P is vital for the release of glucose into the bloodstream from _____ breakdown.
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Glycogen (glycogenolysis)
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Where does glucose-6-phosphatase break glycogen stores?
|
Liver not muscle
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Glucose that is released from glycogen stores of the muscle will be _____ in the glycolytic pathway
|
oxidized
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A biochemical process in which glucose is made from molecules that are not carbohydrates (primarily from amino acids but not fatty acids).
Where does this process take place? |
Gluconeogenesis
Liver |
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Typically gluconeogenesis involves the conversion of lactic acid or amino acid into _____ or _____, which is then converted to glucose.
|
Pyruvate
phosphoenolpyruvate |
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What does Pyruvate carboxylse catalyze?
|
Pyruvate - oxaloacetate
|
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What does phosphoenolpyruvate carboxykinase catalyze?
|
Oxaloacetate - phosphoenolpyruvate
|
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What does fructose-1,6-bisphosphase catalyze?
|
Fructose-1,6-bisphosphate - fructose-6-phosphate
|
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What does glucose-6-phosphatase catalyze?
|
glucose-6-phosphate - glucose
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Glucose-6-phosphatase does/does not contain a high-energy bond.
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Does not
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The Michaelis constant is = the _____ _____ at which Vo (_____ _____ _____) is one-half Vmax.
What are the units? |
Substrate conc.
Initial reaction velocity Molarity |
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What are the ranges of Km?
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10^-1 and 10^-6 M
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What does the Km value of an enzyme depend on?
|
Particular substrate
Environmental conditions |
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The _____ the Km the _____ the relative affinity.
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Lower
Higher |
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The Km values for enzyme-substrate reactions increase in the presence of a _____ _____.
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Competitive inhibitor
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Km values for enzyme-substrate reactions are not affected in the presence of a noncompetitive inhibitor; however, _____ is reduced.
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Vmax
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What is obtained when the enzyme sites are saturated with substrate?
|
Maximal rate (Vmax)
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Allosteric enzymes usually show a complex relationship between the _____ and _____ _____.
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Velocity
Substrate Concentration |
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What are the 2 mechanisms acting on enzymes which regulate metabolic processes?
|
Allosteric modification
Covalent modification |
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An allosteric enzyme is a regulatory is a regulatory enzyme and has both an active site for _____ and an allosteric site for _____.
|
Substrate
Effector |
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A substrate binds to the active site when what is absent?
What has a higher binding potential than the substrate? What causes conformational changes on a protein which thereby changes its active site? |
Effector
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Those binding aspects on a protein which increase catalytic activity.
|
Positive effector
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Those binding aspects on a protein which decreases catalytic activity.
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Negative effector
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What is the reversible covalent modification of an enzyme
|
Covalent modification
|
|
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What is the most common form of covalent modification?
|
Enzyme phosphorylation
|
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What groups does phosphorylation occur on?
|
Ser-OH
Thr-OH Tyr-OH |
|
|
What are the two states that an enzyme exists in?
|
Phosphorylated
Unphosphorylated or Active Inactive |
|
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What is enzyme phosphorylation catalyzed by ?
|
ATP-dependent protein kinases
|
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How are phosphorylated enzymes dephosphorylated?
|
By phosphoprotein phosphatases
|
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What is the substrate for glycogen synthesis?
|
UDP Glucose
and non-reducing end of glycogen |
|
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What is the enzyme which carry's out the synthesis of glycogen?
|
Glycogen synthase
|
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Glycogen synthase is responsible for making the _____ linkages in glycogen.
|
1,4
|
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What is glucose initially phosphorylated by in most tissues for glycogen synthesis?
|
Hexokinase
|
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What is glucose initially phosphorylated by in the liver for glycogen synthesis?
|
Glucokinase
|
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What initiates glycogen synthesis?
What enzyme does this? |
glucose-6-phosphate <--> glucose-1-phosphate
phosphoglucomutase |
|
|
What is glucose-1-phosphate converted to in the second step of gylcogen synthesis?
What enzyme does this? |
UDP-Glucose
UDP-Glucose pyrophosphorylase |
|
|
Of the glycogen synthases what is the active enzyme and is the dephosphorylated form?
|
Glycogen Synthase A
|
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Of the glycogen synthases what is the inactive form and is the phosphorylated form?
|
Glycogen Synthase B
|
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|
What breaks down glycogen?
What are its forms? |
Glycogen phosphorylase
A and B |
|
|
What is the phosphorylated form of glycogen phosphorylase which forms an active enzyme?
Where does this happen? |
Glycogen phosphorylase A
Liver cells |
|
|
What is the dephosphorylated form of glycogen phosphorylase which forms the inactive enzyme?
|
Glycogen phosphorylase B
|
|
|
Where are Glycogen synthase and glycogen phosphorylase phosphorylated at?
|
Specific Serine residues
|
|
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What is the protein which is located at the core of the glycogen molecule?
|
glycogenin
|
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When an inhibitor resembles the substrate and binds to the active site of the enzyme. The substrate is then prevented from binding to the same active site.
|
Competitive Inhibitor
|
|
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What is the hallmark of competitive inhibition?
|
Can be overcome by increasing amounts of substrate
|
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When an inhibitor and substrate can bind simultaneously to an enzyme molecule. This means that their binding sites _____ _____ overlap.
|
Noncompetitive inhibition
|
|
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Becuase the inhibitor and substrate do not compete for the same site, noncompetitive inhibitor _____ be overcome by increasing the substrate concentration.
|
Cannot
|
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A noncompetitive inhibitor is by definition an _____ inhibitor.
|
Allosteric
|
|
|
Inhibition where the inhibitor and substrate bind at different sites which do not overlap.
|
Uncompetitive inhibition
|
|
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What is the hallmark of uncompetitive inhibition?
|
Inhibitor only binds to the enzyme only when a substrate is already attached (ES Complex)
|
|
|
What are the reversible inhibitors?
|
Competitive inhibition
Noncompetitive inhibition Uncompetitive inhibition |
|
|
______ inhibitors are those that combine with or destroy a functional group on the enzyme that is essential for its activity.
|
Irreversible
|
|
|
What is a classic example of irreversible inhibition?
|
Aspirin inhibition of cyclooxygenase
(Acetylates active site serine) |
|
|
What are the characteristics of competitive inhibition?
|
- Overcome by increasing substrate
- Vmax stays same - Km increased |
|
|
What are the characteristics of noncompetitive inhibition?
|
- Is not overcome by increasing substrate
- Vmax decreased - Km unchanged |
|
|
The rate at which an enzyme works is influenced by what factors?
|
Concentration of substrate
Temp. Inhibitor presence pH |
|
|
Increased concentration _____ enzyme rate
Increased temp. _____ enzyme rate Increased inhibitor _____ enzyme rate |
Increased
Increased (Until upper limit reached) Decreased |
|
|
Trypsinogen is converted to Trypsin by what enzyme?
|
Enteropeptidase
|
|
|
The presence of amino acids in the small intestine (es. duodenum) stimulates the release of what?
In turn what does this cause a release of? |
Cholecystokinin
Pancreatic Zymogens and Gall bladder contraction |
|
|
_____ can act as an activator for all zymogens of pancreatic proteases
|
Trypsin
|
|
|
What are the specific zymogens that trypsin converts into an active form?
|
Trypsinogen
Chemotrypsinogen Proelastase Procarboxypeptidase A and B |
|
|
What is secreted by chief cells in the stomach and activated by low pH or other activating _____ molecules?
|
Pepsinogen
Pepsin |
|
|
What cleaves peptide bonds in which the carboxyl group is contributed by lysine and arginine (basic amino acids)?
|
Trypsin
|
|
|
What cleaves peptide bonds in which the carboxyl group is contributed by the aromatic amino acids or by leucine?
|
Chymotrypsin
|
|
|
What cleaves at the carboxyl end of amino acid residues with small, unchanged side chains such as alanine, glycine, or serine?
|
Elastase
|
|
|
What has little activity on aspartate, glutamate, arginine, lysine, or proline?
|
Carboxypeptidase A
|
|
|
What cleaves basic amino acids, lysine, and arginine?
|
Carboxypeptidase B
|
|
|
What refers to any of a large group of enzymes that catalyze the hydrolysis of peptide bonds in the interior of a polypeptide chain or protein molecule?
|
Endopeptidase
|
|
|
What enzyme is used as an indicator of osteoblastic activity?
|
Alkaline phosphatase
or Osteocalcin |
|
|
What is the second most abundant bone matrix protein used in bone after type 1 collagen?
|
Osteocalcin
|
|
|
What is believed to increase the local concentration of inorganic phosphate or to activate the collagen fibers in such a way that they cause the deposition of _____ salts?
|
Alkaline phosphatase
Calcium |
|
|
Alkaline phosphatase is involved in bone _____ and hydrolysis of _____ _____.
What pH does it function at? |
Mineralization
Phosphoric esters 8.6 |
|
|
_____ are any group of enzymes that liberate inorganic phosphate from phosphoric esters.
|
Phosphatases
|
|
|
What are two examples of phosphatases?
|
Alkaline phosphatase
Acid phosphatase |
|
|
What diseases are high levels of alkaline phosphatase seen?
Low Levels? |
Paget's bone disease and Osteosarcomas
Hypophosphatasia |
|
|
A phosphatase with optimum functioning at pH 4.5 and is present in the prostate gland.
|
Acid phosphatase
|
|
|
What is an inorganic compound found in muscle tissue and capable of storing and providing energy for muscular contraction?
|
Creatine phosphate
|
|
|
What is a phosphate molecule which plays a secondary role in bone development?
|
Pyrophosphate
|
|
|
Apoenzyme + cofactor = ?
|
Haloenzyme
|
|
|
What is the cofactor for the enzymes:
Cytochrome oxidase Catalase Peroxidase Ferredoxin? |
Fe2+, Fe3+
|
|
|
What is the cofactor for the enzymes:
Cytochrome oxidase Pyruvate phosphokinase? |
Cu2+
|
|
|
What is the cofactor for the enzymes:
Carbonic anhydrase Alcohol dehydrogenase? |
Zn2+
|
|
|
What is the cofactor for the enzymes:
Hexokinase Glucose-6-phosphatase Pyruvate kinase? |
Mg2+
|
|
|
What is the cofactor for the enzymes:
Arginase Ribonucleotide reductase? |
Mn2+
|
|
|
What is the cofactor for the enzymes:
Pyruvate? |
K+
|
|
|
What is the cofactor for the enzymes:
Urease? |
Ni2+
|
|
|
What is the cofactor for the enzymes:
Dinitrogenase? |
Mo
|
|
|
What is the cofactor for the enzymes:
Glutathione peroxidase? |
Se
|
|
|
What functions as a coenzyme that is vital to tissue respiration?
|
Thiamine pyrophosphate
|
|
|
Thiamine pyrophosphate is required as a cofactor for the enzyme _____ _____, which catalyzes the oxidative decarboxylation of _____, to form _____, which then enters into the _____ _____ for the generation of energy.
|
Pyruvate dehydrogenase
Pyruvate Acetyl-CoA Kebs Cycle |
|
|
Thiamine pyrophosphate is also a coenzyme for _____, which functions in the _____ _____ _____, and alternate pathway for glucose oxidation.
|
Transketolase
Pentose phosphate pathway |
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What coenzyme functions in certain oxidation / reduction reactions in the body?
What is it derived from? |
Flavin adenine dinucleotide (FAD)
Riboflavin (Vitamin B2) |
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What coenzyme is utilized alternatively with NADH as an oxidizing or reducing agent in various metabolic processes?
What is it derived from? |
Nicotinamide adenine dinucleotide (NAD)
Nicotinic acid (niacin) |
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What coenzyme functions as an acyl group carrier and is necessary for fatty acid synthesis and oxidation, pyruvate oxidation, and other acylation reactions?
What is it derived from? |
Coenzyme A
Pantothenic Acid (vitamin B3) |
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What coenzyme is essential for many enzymatic reactions, almost all of which are associated with amino acid metabolism?
What is it derived from? |
Pyridoxal phosphate (PLP)
Pyridoxine (vitamin B6) |
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What coenzyme participates in the transfer of various carbon fragments from on e molecule to another; they are, for instance, involved in the synthesis of methionine and thymine?
What is it derived from? |
Tetrahydrofolate
Folic Acid |
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What coenzyme is a cofactor for the pyruvate dehydrogenase complex, which breaks down pyruvate to form acetyl-CoA?
What is it derived from? |
Lipoate
Not required in diet |
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What coenzyme is an essential cofactor for several enzymes?
What is it derived from? |
Coenzyme B12
Vitamin B12 |
