Multifunctional enzymes and evolution of biosynthetic pathways: retro-evolution by jumps

Roy, Siddhartha (1999) Multifunctional enzymes and evolution of biosynthetic pathways: retro-evolution by jumps Proteins: Structure, Function, and Bioinformatics, 37 (2). pp. 303-309. ISSN 0887-3585

Full text not available from this repository.

Official URL:

Related URL:<303::AID-PROT15>3.0.CO;2-6


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.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Pathway; Biosynthesis; Evolution; Multifunctional; Enzyme
ID Code:43184
Deposited On:10 Jun 2011 07:37
Last Modified:10 Jun 2011 07:37

Repository Staff Only: item control page