*The enzyme glucose oxidase isolated from the mold Penicilliumnotatum catalyzes the oxidation of 3-D-glucose to D-glucono-6-lactose. This enzyme is highly specific for the ß anomer ofIn spite of thisglucose and does not affect the a anomer.specificity, the reaction catalyzed by glucose oxidase iscommonly used in a clinical assay for total blood glucosethat is, for solutions consisting of a mixture of 3- and a-D-glucose. What are the circumstances required to make thispossible? Aside from allowing the detection of smaller quan-tities of glucose, what advantage does glucose oxidase offerover non-enzymatic oxidizing agents like Tollens reagent?*Is B-D-glucosamine a reducing sugar?

Carbohydrates are polyhydroxy aldehydes or ketones. They can be classified as monosaccharides,…

Answered: *The enzyme glucose oxidase isolated…

Biochemistry

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ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

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Problem 14P: The Energy Cost of dTTP Synthesis (Integrates with Chapter 20.) Starting from HCO3, glutamine,...

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a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-Dglucose to D-glucono-δ-lactone. This enzyme is highly specific for the β anomer of glucose and does not affect the α anomer. In spite of this specificity, the reaction catalyzed byglucose oxidase is commonly used in a clinical assay for total blood glucose—that is, for solutions consisting of a mixture of β- and α-D-glucose. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for measuring blood glucose?
The enzymatic activity of PFK1 is generally measured by set- ting up a coupled enzyme assay system whereby aldolase, triose phos- phate isomerase, and glycerol-3-phosphate dehydrogenase are added to the assay mixture. For the latter enzyme, NADH is added and its change in concentration is readily monitored at 340 nm. Write the chain of reactions catalyzed by these enzymes using structural formulas, label substrates and products, and explain why the coupled en- zyme assay system leads to oxidation of NADH. While the chain of reac- tions is similar to those in glycolysis, there is a critical difference because of the dehydrogenase enzyme. Describe how this enzyme causes the chain of reactions to differ from those in glycolysis.
The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of B-D-glucose to D-glucono-6-lactone. The enzyme is highly specific for the B anomer of glucose and does not affect the a anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose -that is, for solutions consisting of a mixture of B- and a-D-glucose, as well as other sugars present in blood. The oxidation proceeds in the presence of oxygen and forms hydrogen peroxide, in addition to the lactone. A second enzyme, called peroxidase, catalyzes the reaction of hydrogen peroxide with colorless compounds to create a colored product, which is quantified with a simple spectrophotometer. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over the Fehling's reagent for measuring blood glucose?
The specific activity of a pure preparation of pyruvate kinase (PK) assayed in the direction of pyruvate formation (forward direction) is 220 U/mg at 25 C and at pH 7.5. This form of PK is a homotetramer (MW 240,000) with one active site per subunit. What is the kcat for PK in the forward direction?
Glucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.
3. (a) The activity of the Pentose Phosphate Pathway is commonly quantified by measuring 14CO2 production from C-14 labeled glucose. In this assay, glucose is metabolized aerobically by cells or tissue slices; both [1-14C] glucose and [6-14C] glucose are employed separately but in parallel. This classical method, thus, requires two separate assay mixtures. Which radioactive isotopomer of glu- cose releases 14 CO2 generated by the Pentose Phosphate Pathway? Confirm your conclusion by drawing the intermediates of the oxidative phase of the PPP with structural formulas, starting with glucose-6-phosphate. Name the intermediates and indicate enzymes. (b) ( Because the assay protocol requires aerobic incubation of cells or tis- sue slices with isotopically labeled glucose in parallel assays, what is the purpose of the other radioactive glucose derivative? To answer this question base your answer using the diagram on the right. O2 NADH CH₂OH + 2 NAD+ HO HO + 2 Pj 2 CO + 2 ATP HO OH 2 ADP CH3…
3. (a) The activity of the Pentose Phosphate Pathway is commonly quantified by measuring 14CO2 production from C-14 labeled glucose. In this assay, glucose is metabolized aerobically by cells or tissue slices; both [1-14C] glucose and [6-14C] glucose are employed separately but in parallel. This classical method, thus, requires two separate assay mixtures. Which radioactive isotopomer of glu- cose releases 14 CO2 generated by the Pentose Phosphate Pathway? Confirm your conclusion by drawing the intermediates of the oxidative phase of the PPP with structural formulas, starting with glucose-6-phosphate. Name the intermediates and indicate enzymes. (b) ( Because the assay protocol requires aerobic incubation of cells or tis- sue slices with isotopically labeled glucose in parallel assays, what is the purpose of the other radioactive glucose derivative? To answer this question base your answer using the diagram on the right. O + 2 NADH CH₂OH + 2 NAD+ ○ HO HO + 2 Pi 2 CO + 2 ATP HO OH 2 ADP…
Multivitamin B complex are essential compounds that are used as derivatives for compounds necessary for many metabolic activities. Give 3 vitamin B compounds and explain where and how they are used along the metabolic pathway.
The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.
ALANINE AMINOTRANSFIRASE AND ASPARTATE AMINOTRANSFERASE (KARMEN МЕТHOD) (C. chemistry) 1. state the reason why substrate must be incubated prior to the addition of serum 2. what part of the steps need extra to avoid positive results? 3. describe the principle of AST/ALT kinetic method.
The activity of the enzyme β-galactosidase produced bywild-type cells grown in media supplemented with different carbon sources is measured. In relative units, thefollowing levels of activity are found:Glucose Lactose Lactose + glucose0 100 1Predict the relative levels of β-galactosidase activity incells grown under similar conditions when the cells arelacI−, lacIS, lacO+, and crp−.

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