The relative enzymatic activity of GS monomers should be predicted. Concept Introduction: Glutamine synthetase (GS) (EC six.3.1.2) is a protein that plays an important role within the microorganism. GS are dodecamers with twelve active sites between every compound. Every substance will scale back the activity of the enzyme; once all final aminoalkanoic acid metabolites are certain to GS, the activity of GS is sort of utterly restrained.

Question

Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. The mammalian enzyme is tetrameric, negatively regulated by both Fructose 2,6-bisphosphate and AMP. Propose three (3) distinct models for how these molecules regulate FBPase activity. Also, describe how the enzyme might differentiate between Fructose 1,6 bisphosphate and Fructose 2,6-bisphosphate binding to the allosteric site on the enzyme with particular emphasis on amino acids comprising the allosteric binding site(s).

Answer 1

Question

Chapter 25, Problem 19P

Interpretation Introduction

Interpretation:

The relative enzymatic activity of GS monomers should be predicted.

Concept Introduction:

Glutamine synthetase (GS) (EC six.3.1.2) is a protein that plays an important role within the microorganism. GS are dodecamers with twelve active sites between every compound. Every substance will scale back the activity of the enzyme; once all final aminoalkanoic acid metabolites are certain to GS, the activity of GS is sort of utterly restrained.

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