Some Evolutionary Relationships of the Primary Biological Catalysts Glutamine Synthetase and RuBisCO
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Excerpt
The polypeptide folds of two primary biological catalysts have been determined by X-ray crystallography. One is glutamine synthetase (GS) from Salmonella typhimurium, which catalyzes the entry of nitrogen into metabolism, and the other is ribulose bisphosphate carboxylase/oxygenase (RuBisCO) from tobacco, which catalyzes the entry of carbon into metabolism. Both are oligomeric structures having complicated patterns of interdomain and intersubunit contacts.
In this paper we consider three questions: (1) What are the patterns of folding of polypeptide chains in GS and RuBisCO, and how do the folded domains interact in the oligomeric enzyme? (2) Which features of the folding patterns are conserved in distantly related species and which are changed? and (3) What do the patterns of conservation and change tell us about the evolution of these catalytic functions?
Both GS and RuBisCO are primary biological catalysts in the sense that they catalyze the first steps at which nitrogen and carbon,...
