Sections The unstable compound that is formed when the disaccharide maltose binds with the active site of the enzyme maltase is called 4) The binding of ATP with the enzyme pyruvate kinase results in this enzyme's failure to catalyze the last step in the breakdown of glucose during the process of glycolysis. In this situation, ATP acts as the of pyruvate kinase. 5) A particular chemical reaction will only proceed if the particles of its reactants possess energy that is greater than 250 kilojoules per mole (kJ/mol). 250 kJ/mol is the for this reaction. 6) Many of the enzymes involved in photosynthesis aid in chemical reactions that remove electrons from the oxygen atoms in water and transfer these electrons to the carbon atoms in carbon dioxide. Based on the kind of reaction that they catalyze, these enzymes are classified as 7) Based on where they perform their functions, the enzymes amylase and maltase in humar saliva are classified as monosaccharides glucose and galactose, lactose must first bind to of the enzyme. 8) In order for the enzyme lactase to catalyze the digestion of lactose into t rin, An in prop

Sections The unstable compound that is formed when the disaccharide maltose binds with the active site of the enzyme maltase is called 4) The binding of ATP with the enzyme pyruvate kinase results in this enzyme's failure to catalyze the last step in the breakdown of glucose during the process of glycolysis. In this situation, ATP acts as the of pyruvate kinase. 5) A particular chemical reaction will only proceed if the particles of its reactants possess energy that is greater than 250 kilojoules per mole (kJ/mol). 250 kJ/mol is the for this reaction. 6) Many of the enzymes involved in photosynthesis aid in chemical reactions that remove electrons from the oxygen atoms in water and transfer these electrons to the carbon atoms in carbon dioxide. Based on the kind of reaction that they catalyze, these enzymes are classified as 7) Based on where they perform their functions, the enzymes amylase and maltase in humar saliva are classified as monosaccharides glucose and galactose, lactose must first bind to of the enzyme. 8) In order for the enzyme lactase to catalyze the digestion of lactose into t rin, An in prop

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
The following is the chemical structure of nicotinamide adenine dinucleotides, a coenzyme commonly used in enzymatic reactions. Но 4 HO 0-P-0 *Na "O. `NH2 N 1 "OH H2N OH Which of the indicate regions is the site of the redox activity of this coenzyme? 2.
Consider the mechanism of enolase, as indicated below. Which of the following correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi- select question). Mg2+ Mg2 Enolase PO3- OH -C-C-H H OH HO H-N-H Lys 345 Glu211 2-Phosphoglycerate bound to enzyme Mg2+ Mg2 PO3- OH C-C-H OH HO H H-N*-H Lys 345 O Glu211 Enolic intermediate HOH PO3- H Phosphoenolpyruvate The metal ion (Mg2+) is helping to stabilize the extra negative charge that developed on the carboxyl group in the enolic intermediate. The metal ion (Mg2+) is serving as a general base, removing a proton in order to improve the quality of the nucleophile. The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through metal ion catalysis. The metal ion (Mg2+) is helping to orient the substrate properly in the active site. The metal ion (Mg2+) is accepting a proton in order to improve the quality of the leaving group.
The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
Acid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostrate gland. The enzyme from the prostrate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostrate gland. Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in human blood serum?
Acid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters as follows in the picture Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostate gland. The enzyme from the prostate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostate gland.Tartrate ion can strongly inhibit the phosphatase from the prostate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum?
In the given reaction below, the amino acid NH₂ KMTs undergoes CH3 H3C-N* CH3 reaction.
Figure 1 shows the catalytic triad of a-chymotrypsin. Identify A, B and C. Describe the subsequent steps of stage 1 and stage 2 of a- chymotrypsin mechanism. Illustrate with diagrams. A B CH2 H-N N: H-O Figure 1
The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D
The biosynthesis of vitamin D₂ is a two-step reaction, requiring two types of concerted pericyclic reactions. Draw in the arrows for each step and identify the structure of precalciferol. If an electrocyclic reaction is required, identify if it occurs through a conrotatory or disrotatory reaction. HO H H ergosterol hv precalciferol Cast HO ergocalciferol
Which of the following statement is FALSE ? pKa values of active site residues can be shifted from typical pKa values Enzymes increase Keq Near attack complexes have reacting molecules close enough to form Va der Waals contacts The transition state contains at least one partial bond. QUESTION 12 The angle o in a peptide best describes: O the angle between the two peptide bonds O the angle between the alpha carbon (Ca) and the amide O the angle between the alpha carbon (Ca) and the carbonyl O the angle between the alpha carbon (Ca) and its side chain QUESTION 13 Investigating how protein subunits come together studies: super- secondary structure Click Save and Submit to save and submit. Click Save All Ansuers to save all anscers 7977 Mostly cloody
In addition to O, binding, changes in other chemical conditions can result in hemoglobin changes. pH is one of those factors. It can be understood by reaction #1. Red blood cells have the enzyme Carbonic Anhydrase which catalyzes reaction #2. Using the two reactions explain how pH contributes to the transfer of O2 from the lungs to the tissues. H-Hb* + O2 Hb-O2 + H* Reaction #1 CO2(aq) + H2O= H* + HCO3 Reaction #2