Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Related questions
Question
How does the reaction catalyzed by GAPDH from T. tenax presented here differ from the reaction carried out in E. coli?
Transcribed Image Text:Introduction: Carbohydrate metabolism in the thermophilic archaeum Thermoproteus
tenax is peculiar compared to the types of organisms usually studied in biochemistry. For
example, the phosphofructokinase reaction in T. tenax is reversible, and is dependent on
pyrophosphate (PP;) rather than isoenzymes. One is well known, and, although it requires
NADP as a cofactor instead of NAD*, it resembles the GAPDH enzyme studied in class,
and is referred to as the "phosphorylating GAPDH”.
In contrast, the second isoenzyme is irreversible and requires NAD*, and is referred to as
the "nonphosphorylating GAPDH". In this case study, we will consider the properties of
this latter enzyme. The balanced equation of the reaction catalyzed by the
nonphosphorylating NAD*-dependent GAPDH is:
H
-H
-C-OHDO al
CHO
NAD*
of Glyceraldehyde-3-phosphate bedw
GAPDH
T. tenax
-0-6
H-C-OH
H₂C-0-
3-phosphoglycerate
+ NADH + H*
-0
T. tenax stores energy in the form of glycogen, which is converted to glucose-1-
phosphate. The G1P is then converted to glucose-6-phosphate and enters the glycolytic
pathway. The two GAPDH enzymes are probably differently regulated in T. tenax. The
authors of this study propose that the phosphorylating, NADP-dependent GAPDH is
involved in efficient ATP production, whereas the non-phosphorylating, NAD*-
dependent GAPDH is somewhat involved in ATP production but is also involved in
providing intermediates for cellular biosynthetic reactions.
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution
Trending nowThis is a popular solution!
Step by stepSolved in 3 steps
Knowledge Booster
Similar questions
- Nitrogenase complexes are irreversibly inactivated by oxygen. Explain how nitrogen-fixing bacteria solve this problem.arrow_forwardWhat are the structural elements that are required for proper function in yeast alcohol dehydrogenase ADH1?arrow_forwardDraw the mechanism of action of an HIV protease. Label the substrate, the intermediates, and the products. Indicate each type of catalysis that occurs throughout the mechanism..arrow_forward
- What bacterial phyla are known to contain dissimilativesulfate-reducers?arrow_forwardWhich step is catalyzed by the enzyme responsible for the Met 2 mutant? (picture attached) A) homoserine → cysteine B) cysteine → cystathionine C) cystathionine → homocysteine D) homocysteine → methionine E) methionine → homoserinearrow_forwardHow does the loss of the Adenomatous polyposis coli (APC) protein lead to the deregulation of Beta-catenin functions in FAP patients?arrow_forward
- A number of auxotrophic mutant strains were isolated from wild-type haploid Neurospora crassa. These strains responded to the addition of certain nutritional supplements to minimal culture medium either by growth (+) or no growth (0) The data from this experiment are presented in the table below. Diagram a biochemical pathway, complete with positions of intermediates, that is consistent with the data. Indicate where in the pathway each mutant strain is blocked.arrow_forwardwhat is meant by S195? D102? H57? What do you figure would happen to the enzymes catalytic activity if the amino acids above were mutated?arrow_forward
arrow_back_ios
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON