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Biomolecules and Metabol

by: Charity Daniel

Biomolecules and Metabol BIS 105

Charity Daniel
GPA 3.76

Kenneth Hilt

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Kenneth Hilt
Class Notes
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This 5 page Class Notes was uploaded by Charity Daniel on Tuesday September 8, 2015. The Class Notes belongs to BIS 105 at University of California - Davis taught by Kenneth Hilt in Fall. Since its upload, it has received 388 views. For similar materials see /class/187631/bis-105-university-of-california-davis in Biological Sciences at University of California - Davis.

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Date Created: 09/08/15
10f5 Biological Sciences 105 Answer Key Winter 2015 K Hilt Homework 2 Learn the structures enzyme names cofactorcoenzyme requirements and regulation of glycolysis see page 3 Be able to draw the structure of a triglyceride triacylglycerol fat and the phospholipids phosphatidylcholine and phosphatidylserine with any of the five fatty acids attached 160 180 18 19 182912 and 18391215 palmitic stearic oleic linoleic and xlinolenic respectively Assigned problems in Biochemical Calculations Segel 1 Enzymes 44 on pp 223224 and 49 on pp 237238 pp 319 2 3 610 and 12 You need to be able to plot and interpret LineweaverBurk graphs 2 Beer s Law calculations example 54 on page 332 4 on page 352 3 K39eq and AG calculations examples 33 34 and 35 on pages 161 7164 1 Enzyme Z catalyzes the reaction A NAD lt gt B NADH H Besides following the H using a pH meter the reaction can be monitored spectroscopically at 340 nm This is the wavelength at which NADH absorbs light Some of the first enzymes that were worked on in biochemistry were dehydrogenases like our enzyme Z because of this advantage Radioisotopes were not yet available a Diagram what the kinetic assay results would be if the reaction was measured from left to right What would it be if the assay was measured from right to left NADH left to right red line right to left green line Time 20f5 b Describe how you would accurately determine enzyme Z39s Km for NAD Describe the experimental setup and the analysis of data Assay a series of tubes where the concentrations of buffer compound A and enzyme Z were constant Vary the concentration of NAD Make a LineweaverBurk plot and determine the Km from the X intercept lv0 1S c Imagine that twenty IU s of enzyme Z were catalyzing the above reaction for one minute under Vmax conditions in a 300 ml assay volume The assay is buffered with 20 mM phosphate buffer pH 760 What will the pH be at the end of that one minute pH 70 Use two HendersonHasselbalch equations This question is very similar to questions 40 and 41 in Biochemical Calculations Segel on page 93 which were assigned in homework 1 3 of 5 2 You are going to measure the enzyme activity of enzyme T Enzyme T catalyzes the reaction S gt P Enzyme T has a Km of 10 X 10396 M for S You miX the following solutions together 260 ml 10 mM phosphate buffer pH 72 030 ml 30 mM S 010 ml enzyme T The results of this enzyme assay are plotted below nmol P produced in assay Time seconds a What is v0 for the above reaction Take any two points and calculate the slope How many International Units IU s of enzyme T were present in the assay 0030 IU Carefully sketch in on the above graph the expected initial velocity if the substrate concentration had initially been 15 X 10396 M 06 VV Draw a line on the graph with a slope of 18 nmolmin Note this line can begin anywhere but needs to have this slope d Let s assume that 10 X 103912 mol of enzyme T was present in both assays ie in part a and in part c Calculate the turnover number for enzyme T Turnover number k2 30000 min391 Note the turnover number always refers to the optimal velocity ie Vmax optimal substrate concentration optimal pH etc The turnover number for the reverse reaction would be k 1 4of5 3 A student runs an enzyme assay using the anaerobic glycolytic enzyme lactate dehydrogenase LDH Their 1 ml assay is 900 pl 200 mM Tris pH 73 35 pl 30 mM pyruvate in H20 35 ul 66 mM NADH in H20 30 ul of their LDH solution in 200 mM Tris pH 73 They miX everything gently together in a cuvette and then measure the AA340Atime using a spectrophotometer Their measured AA34030 sec was 003 l l a On the enzyme kinetic graph what is plotted on the X and y aXes Refer to your notes b What does the in 003ll tell you The compound that you are measuring is being consumed c How many IU s of LDH were present in the 30 ul that you added ENADH 340 m 6220 M39lcm39l 001 IU You need to make up 500 ml of 200 mM Tris buffer pH 73 in order to run your LDH assays You have a 10 M Tris solution pH 9 and 10 M HCl and 10 M NaOH How will you make up the buffer 100 ml 10 M Tris pH 9 75 ml 10 M HC1 325 ml water e Let s imagine that your LDH enzyme has a Km for NADH of 40 MM and a Vmax of 80 nmoles X liter391 X min39l What would your LineweaverBurk plot look like Draw it Label your X and yaXes using eXponents See gure 413 on page 239 in Biochemical Calculations 50f5 CHCHOH ethanol dawns dEhydxugLmh Glycolysis and Alcoholic Fermentation NAU39 NADH v H acelaldehvde cnrcuo co per Ms ummxvme TPF39 7 NAD39 02 ll ADP ATP HpFo HOH HOH hexnkmase o f mummzlyymngmase pyruvate Glucose CH 5Aphasphale lactate WW A rw ADP LHM l l phosphngmcasu E UEOSE snmerisEWSH moml coz39 OH I Fructose H p asphoenol oPol Srohosphate pvruvale PEP H1 ATP pnmmmxnmmmaze 410 nnmasv ADP Hzopol 0 CH 0P0 mm o z zz ugghagwceraxe H 0 l 16 anpnospnaie 1 140 h vwlmoglyl skin s murase GlyceraldehydeI c I CHZOH 1 phosphate I Dihydruxy 10 0 V m HCOH acetone phosphate H m H10P0 39 C PI NADH op0 10 ADP HOF0 moss phnsphnw c Srphosphoglycerate HCOH Isamfrass m NAD H OH nhnsmmgwty E swan Mum HIOPO mimmehyde 4 phnsphnte Jelvydrogenese 13blsphosphoglycerate The above diagram is adapted from Outlines ofBiochemistry 3rd ed by Eric E Conn andPK Stumpf Professors Conn and Stumpf founded the biochemistry department at UC Davis


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