Title: Glutamine Synthetase of Escherichia Coli: Some Physical and Chemical Properties
Abstract: This chapter discusses the physical and chemical properties of glutamine synthetase. It discusses some aspects of the macromolecular structure of glutamine synthetase from Escherichia coli, together with some interactions of the enzyme with effectors. It also justifies a detailed consideration of the presently known structural features of this enzyme on the basis of glutamine synthetase being a potential model for other allosteric enzymes with multiple catalytic subunits and no regulatory subunits. Without regulatory subunits, the regulation of glutamine synthetase activity in E. coli occurs at the subunit level. Glutamine synthetase plays a central role in the nitrogen metabolism of E. coli because glutamine is an important intermediate in the assimilation of ammonia by this microorganism. The amide nitrogen of glutamine is utilized in the biosynthesis of AMP, CTP, tryptophan, histidine, glucosamine 6-phosphate, carbamyl phosphate, and also L-glutamate. In addition, glutamine synthetase may be coupled with glutamate synthase and various transaminases to provide a pathway for ATP-dependent synthesis of most amino acids. As a consequence, a rigorous cellular control of glutamine synthetase activity in E. coli has evolved.
Publication Year: 1972
Publication Date: 1972-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
Access and Citation
Cited By Count: 84
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot