Which of the following functions describes the enzyme Peptidase? A. remove phosphate from a substrate B. removal of H2O C. cleave phosphodiester bond D. cleave amino bonds
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- MULTIPLE CHOICE - Please answer properly QUESTION : Supposed you want to use phosphoglucomutase to breakdown glycogen. You found out that this enzyme is responsible for converting glucose l-phosphate (C6H1309P) to glucose-6-phosphate (C6H1309P). Based on this action, to which enzyme class does phosphoglucomutase belong? A. Isomerase B. Oxidoreductase C. Lyase D. LigaseBIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligasets.edu.au/courses/26618/quizzes/67363/take Question 14 Select the correct statements. The enzymes used in glycolysis involves __________. Note there might be more than 1 correct statement. e to search U kinases to transfer phosphate groups between ADP and ATP kinases to rearrange carbon bonds in sugar molecules isomerases to phosphorylate sugar molecules hydrolases to rearrange carbon bonds in sugar molecules oxidoreductases to transfer electrons between molecules l 88 16°C G N Paused Upda ENG 10:55 PM
- Instructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________ Name: alkaline phosphatase Reaction: a phosphate monoester + H2O = an alcohol + phosphate _____________________ Reaction: L-threonine = D-threonine. Other information: Inverts both chiral centers, a racemase. _____________________ Name: glycine-N-acylase Reaction: acyl-COA + glycine = CoA + N-acylglycine _____________________ Name: lysine decarboxylase Reaction: L-lysine = cadaverine + CO2 _____________________ Name: methanol dehydrogenase Reaction: methanol + NAD+ = formaldehyde + NADH + H+Instructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________ Name: alkaline phosphatase Reaction: a phosphate monoester + H2O = an alcohol + phosphate _____________________ Reaction: L-threonine = D-threonine. Other information: Inverts both chiral centers, a racemase. _____________________ Name: glycine-N-acylase Reaction: acyl-COA + glycine = CoA + N-acylglycine _____________________ Name: lysine decarboxylase Reaction: L-lysine = cadaverine + CO2 _____________________ Name: methanol dehydrogenase Reaction: methanol + NAD+ = formaldehyde + NADH + H+ _____________________ Name: citryl-CoA synthetase Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA _____________________ Name: D-xylulose reductase Reaction: xylitol + NAD+ = D-xylulose + NADH + H+ _____________________ Name: cellobiose phosphorylase Reaction:…Answer TRUE or FALSE.a. According to the lock-and-key model of enzyme action, the active site of an enzyme is not flexible in shape.b. In an enzyme-catalyzed reaction, the compound that does not undergo a chemical change is called the substrate.c. The nonprotein portion of a conjugated enzyme is not the enzyme’s active sited. Simple enzymes are composed only of protein; conjugated enzymes have nonprotein cofactors.
- Please answer clearly and directly.Give 3 types of specificity of enzyme and an example for each. Example: Relative Specificty - α-amylase enzyme can hydrolyze α-1-4 glycosidic linkage in starch and glycogenI. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.Drag and drop from the available list of terms. are a diverse set of enzyme that catalyze two molecules by forming a new bond in the process. Transferases Kinases joining Lyases Ligases separating Oxidoreductases Dehydrogenases converting hydrolytic
- =display&toolld3calendar-mybb, Gmail YouTube Maps calendar-tool Home Courses C A Question Completion Status: 20 3D 70 100| 11凸|12D|| 130 14 150 16 170 QUESTION 14 A newly isolated bacterial isocitrate dehydrogenase is found to have a molecular mass of 180KDA and SDS-PAGE shows it to be a homodimer. 1mg of enzyme produces 0.05 mmoles of product per minute per mL. What is the turnover number of this enzyme in µmol product produced per pmol of enzyme subunit per mL? O a. 4.5 Ob.4500 O c. 9000 O d.9 QUESTION 15 The absorption spectrum of NAD" and its reduced form NADH are shown below: Absorption 2,4 2,0 1,6 Click Save and Submit to save and submit. Click Save All Answers to save all answers. Save All Ar 8 11 JAN 9. tv W ... LOQuestion:- name the enzyme that is used in this reaction and explain whyavailable. Research an enzyme that is needed in the human body. Address the following topics: 1. Describe the structure of that enzyme. 2. Explain the specific action of that enzyme in the body. 3. What disorders/diseases would you expect if there was a deficiency of this enzyme?