PMID:10584075
| Citation |
Roy, S (1999) Multifunctional enzymes and evolution of biosynthetic pathways: retro-evolution by jumps. Proteins 37:303-9 |
|---|---|
| Abstract |
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 metabolite and availability of another related substance in the environment. In this article, I argue that because of instability of many such extant intermediates, it is unlikely that retro-evolution had occurred in steps. I further propose that such evolution in many cases has taken place by jumps, i.e., by recruitment of a multifunctional enzyme capable of catalyzing several steps at a time, albeit inefficiently. I further speculate that in some cases one primordial multienzyme may have catalyzed the whole sequence of reaction of a biosynthetic pathway, i.e., the pathway may have evolved by a single leap. Gene duplications and further evolution to more efficient enzymes led to extant pathways. Such a mechanism predicts that some or all enzymes of a pathway must have descended from a common ancestor. Sequence and structural homologies among extant enzymes of a biosynthetic pathway have been examined. |
| Links | |
| Keywords |
Amino Acids/biosynthesis; Bacteria/enzymology; Bacteria/metabolism; Catalysis; Diaminopimelic Acid/metabolism; Enzymes/biosynthesis; Enzymes/chemistry; Evolution, Molecular; Methionine/biosynthesis; Models, Biological; Models, Molecular; Protein Structure, Tertiary; Purines/biosynthesis |
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