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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?

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

Biochemistry
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
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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?

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.
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.
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