Structural studies, sequence alignments, and biochemistry have provided new insights into the evolution of the purine biosynthetic pathway. The importance of chemistry, the binding of ribose 5-phosphate (common to all purine biosynthetic intermediates), and transient protein-protein interactions in
Early evolution of the histidine biosynthetic pathway
β Scribed by Renato Fani; Elena Mori; Antonio Lazcano
- Book ID
- 105583923
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 120 KB
- Volume
- 26
- Category
- Article
- ISSN
- 1573-0875
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A likely scenario of evolution of biosynthetic pathways is believed to have occurred by retro-evolution through recruitment of existing enzymes rather than generation of de novo classes. It had been proposed that such retro-evolution occurred in steps as a response to depletion of an essential metab
The hisA and hisF genes belong to the histidine operon that has been extensively studied in the enterobacteria Escherichia coli and Salmonella typhimurium where the hisA gene codes for the phosphoribosyl-5-amino-1 -phosphoribosyl-4-imidazolecarboxamide isomerase (EC 5.3.1.16) catalyzing the fourth s