How does the reaction catalyzed by GAPDH from T. tenax presented here differ from the reaction carried out in E. coli? Introduction: Carbohydrate metabolism in the thermophilic archaeum Thermoproteustenax is peculiar compared to the types of organisms usually studied in biochemistry. Forexample, the phosphofructokinase reaction in T. tenax is reversible, and is dependent onpyrophosphate (PP;) rather than isoenzymes. One is well known, and, although it requiresNADP 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 asthe "nonphosphorylating GAPDH". In this case study, we will consider the properties ofthis latter enzyme. The balanced equation of the reaction catalyzed by thenonphosphorylating NAD*-dependent GAPDH is:H-H-C-OHDO alCHONAD*of Glyceraldehyde-3-phosphate bedwGAPDHT. tenax-0-6H-C-OHH₂C-0-3-phosphoglycerate+ NADH + H*-0T. 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 glycolyticpathway. The two GAPDH enzymes are probably differently regulated in T. tenax. Theauthors of this study propose that the phosphorylating, NADP-dependent GAPDH isinvolved in efficient ATP production, whereas the non-phosphorylating, NAD*-dependent GAPDH is somewhat involved in ATP production but is also involved inproviding intermediates for cellular biosynthetic reactions.

GAPDH (Glyceraldehyde 3-phosphate dehydrogenase) is a glycolytic enzyme. It catalyzes the conversion…

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How does the reaction catalyzed by GAPDH from T. tenax presented here differ from the reaction carried out in E. coli?

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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Question

How does the reaction catalyzed by GAPDH from T. tenax presented here differ from the reaction carried out in E. coli?

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.

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