What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1
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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
- uizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBCThe table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversionsGlucosidase 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.
- Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)Reaction rate 0.35 0.30 0.25 0.20 0.15- 0.10 0.05 0.00 0 1000 2000 Enzyme total is 5mM 3000 4000 1. Substrate concentration 1. The above graph is an enzyme reaction, what is the vMax, KM, and Kcat of this enzymatic reaction? What does vMax, kM and Kcat mean, explain? 2. What are the three forms of regulation that follow the Michaelis Menten kinetics? What are the mechanisms by which these inhibitors can regulate the enzyme?
- Arrange the balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis). First step Last step Answer Bank Fructose 1,6-bisphosphate - dihydroxyacetone phosphate + glyceraldehyde 3-phosphate Fructose 6-phosphate + ATP →→→→ fructose 1,6-bisphosphate + ADP Glucose + ATP → glucose 6-phosphate + ADP Dihydroxyacetone phosphate glyceraldehyde 3-phosphate Glucose 6-phosphate →→→→ fructose 6-phosphateDescribe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the catalysis.Substrate KM (M) N-Acetylvaline ethyl ether 8.8 X 10 -2 N-Acetyltyrosine ethyl ether 6.6 X 10-4 Which substrate has the higher apparent affinity for the enzyme? Explain. Which substrate is likely to give a higher value for Vmax?