D. Describe the effect that each of the following changes would have on the rate of abiochemical reaction involving the substrate arginine and the enzyme arginaseDecreasing the arginine concentrationIncreasing the temperature from itsoptimum value 10°C higher than thisvalueIncreasing the arginase concentrationIncreasing the pH by one unit from itsoptimum value

Enzymes are substances that increase the rate or velocity of a reaction, causing the reaction to…

Answered: D. Describe the effect that each of the…

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter6: Basic Clinical Chemistry

Section6.1: Introduction To Clinical Chemistry

Problem 14RQ

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B. Describe the function implied by the name of each of the following enzymes 1. Citrate decarboxylase 2. Adenine diphosphate phosphorylase 3. Oxalate reductase 4. Nitrite oxidase 5. cis-trans isomerase
C. What types of inhibitors of this enzyme is shown below? [1]. D. What effect (increase, decrease, stay the same) does the inhibitor have on Vmax? E. What effect (increase, decrease, stay the same) does the inhibitor have on Km?
d. Which of the substrates is likely to have a higher Vmax. What is your reasoning? e. Can you propose a molecule that might act as an inhibitor to this reaction? Explain your reasoning.
a. How to distinguish fresh fish? Do you think this has anything to do with the biochemical changes that occur when a fish is caught or harvested? Explain briefly b.What are the signs of cooked fish and shellfish. Explain
Name: Date: Year/Section: Score: ACTIVITY 5.1.1 Determine the catalytic power of jack bean urease in catalyzing the hydrolysis of urea given the following conditions: At 20C, the rate constant for enzyme-catalyzed reaction is 3x104/sec The rate constant for the uncatalyzed hydrolysis of urea is 3x10-10/sec. ACTIVITY 5.1.2 Give examples of enzymatic reaction for each type of specificity 96 Copyright 2019. All Rights Reserved. 2--------
A. Give a systematic name for the enzyme that would act on each of the following substrates 1. Methylamine 2. Glucose-6-Phosphate 3. Citrate 4. Glucocerebroside 5. Hydrogen peroxide
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
a. Complete the reaction below by providing A, B, C and D b. To which other family of amino acids is the family is the family depicted above linked? Which amino acid links these families? c. Which amino acids from the group above is linked to acute lymphoblastic leukemia?
A. Describe the importance of nucleotide metabolism for cells. B. Explain the main features of de novo pathway and salvage pathway of nucleotidemetabolism
Q: part c This is related to biochemical engineering subject
C.. The formation of a hydrogen bonding dimer of N-methylacetamide has been studied as a model for hydrogen bonding in proteins. The thermodynamic parameters (at 298 K) measured for this process in water are shown below. 2 H3C-N H N-methylacetamide CH3 H3C HN CH3 HN CH3 AG° = 3.1 kcal mol-1 AH° 0.0 kcal mol-1 AS° -10 cal mol-1 K-1 H3C N-methylacetamide hydrogen-bonded dimer a) Provide a molecular level reasoning for the value of AH° and sign of ASO for this process. b) The conclusion below may be drawn from these data. Explain how his conclusion is reached. Hydrogen bonds are unlikely to be a strong stabilizing factor for a protein folding in water. c) Do you agree with this conclusion? What might be a limitation of this model for describing protein folding? d) It is well known that hydrogen bonds are prevalent in folded protein structures, so they appear to be important. So, if this conclusion is correct, what is an alternative possible role of hydrogen bonds in protein folding?
explain the phenylketonuria disease mechanism

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