The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 µmol of pyrophosphate in 15 minutes. The purified enzyme has a Vmax of 2800 U per milligram of enzyme. When [S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vmax = If each enzyme subunit has one active site, how many micromoles of active sites, or [E]T, are there in 1 mg of enzyme? [E]T = What is the turnover number, or keat, of the enzyme? μmol. s-¹.mg-¹ Kcat = μmol. mg -1 $1
The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 µmol of pyrophosphate in 15 minutes. The purified enzyme has a Vmax of 2800 U per milligram of enzyme. When [S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vmax = If each enzyme subunit has one active site, how many micromoles of active sites, or [E]T, are there in 1 mg of enzyme? [E]T = What is the turnover number, or keat, of the enzyme? μmol. s-¹.mg-¹ Kcat = μmol. mg -1 $1
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
Problem 1P
Related questions
Question
C7 Q11:
![The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a
pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical
subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 µmol of pyrophosphate in
15 minutes. The purified enzyme has a Vmax of 2800 U per milligram of enzyme.
When [S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second?
Vmax =
If each enzyme subunit has one active site, how many micromoles of active sites, or [E]T, are there in 1 mg of enzyme?
[E]T =
What is the turnover number, or keat, of the enzyme?
μmol. s-¹.mg-¹
Keat =
μmol. mg-¹
81](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc94cb5d1-997a-49d0-b0ef-9ec02bf0a187%2F7d0db86f-31be-4c2b-b885-b20606002808%2F1t3vdhl_processed.png&w=3840&q=75)
Transcribed Image Text:The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a
pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical
subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 µmol of pyrophosphate in
15 minutes. The purified enzyme has a Vmax of 2800 U per milligram of enzyme.
When [S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second?
Vmax =
If each enzyme subunit has one active site, how many micromoles of active sites, or [E]T, are there in 1 mg of enzyme?
[E]T =
What is the turnover number, or keat, of the enzyme?
μmol. s-¹.mg-¹
Keat =
μmol. mg-¹
81
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