Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
Question
Book Icon
Chapter 9, Problem 15P
Interpretation Introduction

Interpretation:

The catalytic powers for subtilisin and carbonic anhydrase should be calculated.

Concept introduction:

The catalytic power of an enzyme can be found by,

Catalytic power = Rate of the enzyme catalyzed reactionRate of uncatalyzed reaction

Blurred answer
Students have asked these similar questions
kcat = ? an enzyme has an aspartic acid in the active site with a pKa = 4.0 and the kcat for this enzyme is directly proportional to the fraction of this side chain that is ionized. If the kcat at pH = 4.0 is 52.9x103 s-1 what is the kcat for this enzymes at pH 3.5
Serine protease enzyme mutation   To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid   Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surely
Chymotrypsin information about enzyme? Trivial/Common Name Systematic (EC) name and number Chemical reaction catalyzed Metabolic pathway Function and cellular localization Size (kDa) and structure (tertiary and quaternary) pH stability Kinetic properties (Km- and Kcat value/s for natural substrates) Stability and potential inhibitors
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning