The Michaelis-Menten parameters, kcat and KM, for selected enzymes are given in the table below. Use these parameters to determine the catalytic efficiency of each enzyme. Based on your calculations arrange the enzymes in increasing order of their efficiencies. Enzyme Substrate Reaction Catalase H₂O2 Urease Urea Acetylcholinesterase Acetylcholine 2-trans-enoyl- COA Crotonase Triose phosphate isomerase Lowest Glyceraldehyde Glyceraldehyde 3-phosphate+ Triosephosphate isomerase 3-phosphate Rank from lowest to highest catalytic efficiency. To rank items as equivalent, overlap them. View Available Hint(s) 2H₂O2 + Catalase 2H₂O + 02 H₂N-C(=O)-NH2 + 2H₂O + Urease → 2NH4+ + CO3²- Acetylcholine + Acetylcholinesterase acetate + choline 2-trans-enoyl-CoA + Crotonase - 3-hydroxyl-CoA + H₂O Crotonase Catalase Triosephosphate isomerase Urease The correct ranking cannot be determined. Keat (S-1) KM (M) 4.0 × 107 1.1 1.0 x 104 2.5 x 10-2 1.4 x 104 9.0 x 10-5 5.7 x 10³ 2.0 x 10-5 Dihydroxyacetone phosphate 4.3 x 10³ 4.7 x 10-4 Acetylcholinesterase Reset Help Highest

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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8L.16.4

The Michaelis-Menten parameters, kcat and KM, for selected enzymes are given in the table below. Use these parameters to determine the catalytic efficiency of
each enzyme. Based on your calculations arrange the enzymes in increasing order of their efficiencies.
Enzyme
Reaction
Catalase
Substrate
H₂O2
Urease
Urea
Acetylcholinesterase Acetylcholine
2-trans-enoyl-
COA
Crotonase
Triose phosphate
isomerase
Glyceraldehyde
3-phosphate
Lowest
Rank from lowest to highest catalytic efficiency. To rank items as equivalent, overlap them.
► View Available Hint(s)
2H₂O2 + Catalase → 2H₂O + O2
H₂N-C(=O)-NH2 +2H₂O + Urease → 2NH4+ + CO3²-
Acetylcholine + Acetylcholinesterase acetate + choline
2-trans-enoyl-CoA +Crotonase →→→ 3-hydroxyl-COA + H₂O
Glyceraldehyde 3-phosphate + Triosephosphate isomerase → Dihydroxyacetone phosphate 4.3 × 10³ 4.7 × 10¯
-4
Crotonase Catalase Triosephosphate isomerase Urease
The correct ranking cannot be determined.
1.1
kcat (S-¹) KM (M)
4.0 × 107
1.0 × 104 2.5 × 10-²
1.4 x 104 9.0 × 10-5
-2
5.7 × 10³ 2.0 × 10-5
Acetylcholinesterase
Reset
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Highest
Transcribed Image Text:The Michaelis-Menten parameters, kcat and KM, for selected enzymes are given in the table below. Use these parameters to determine the catalytic efficiency of each enzyme. Based on your calculations arrange the enzymes in increasing order of their efficiencies. Enzyme Reaction Catalase Substrate H₂O2 Urease Urea Acetylcholinesterase Acetylcholine 2-trans-enoyl- COA Crotonase Triose phosphate isomerase Glyceraldehyde 3-phosphate Lowest Rank from lowest to highest catalytic efficiency. To rank items as equivalent, overlap them. ► View Available Hint(s) 2H₂O2 + Catalase → 2H₂O + O2 H₂N-C(=O)-NH2 +2H₂O + Urease → 2NH4+ + CO3²- Acetylcholine + Acetylcholinesterase acetate + choline 2-trans-enoyl-CoA +Crotonase →→→ 3-hydroxyl-COA + H₂O Glyceraldehyde 3-phosphate + Triosephosphate isomerase → Dihydroxyacetone phosphate 4.3 × 10³ 4.7 × 10¯ -4 Crotonase Catalase Triosephosphate isomerase Urease The correct ranking cannot be determined. 1.1 kcat (S-¹) KM (M) 4.0 × 107 1.0 × 104 2.5 × 10-² 1.4 x 104 9.0 × 10-5 -2 5.7 × 10³ 2.0 × 10-5 Acetylcholinesterase Reset Help Highest
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