The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa), and has one identical active site located on each of its four subunits. You have performed a series of enzyme kinetic experiments using 0.025 mL of an enzyme sample that is 4.0 µg/mL and determined that the following Vmax = 2.442 x 102umoles/min What is the turnover number of this enzyme (in units of #/sec)?

Principles of Instrumental Analysis
7th Edition
ISBN:9781305577213
Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Chapter30: Capillary Electrophoresis, Electrochromatography, And Field-flow Fractionation
Section: Chapter Questions
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The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa), and has one identical
active site located on each of its four subunits. You have performed a series of enzyme kinetic experiments using 0.025
mL of an enzyme sample that is 4.0 pg/mL and determined that the following Vmax = 2.442 x 10-2umoles/min
What is the turnover number of this enzyme (in units of #/sec)?
76/ sec
305 / sec
152 / sec
4579/ sec
1526 / sec
O O O O
Transcribed Image Text:The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa), and has one identical active site located on each of its four subunits. You have performed a series of enzyme kinetic experiments using 0.025 mL of an enzyme sample that is 4.0 pg/mL and determined that the following Vmax = 2.442 x 10-2umoles/min What is the turnover number of this enzyme (in units of #/sec)? 76/ sec 305 / sec 152 / sec 4579/ sec 1526 / sec O O O O
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