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• W2012193456 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. Proteins 1999;37:303–309. ©1999 Wiley-Liss, Inc." @default.
• W2012193456 created "2016-06-24" @default.
• W2012193456 creator A5046416885 @default.
• W2012193456 date "1999-11-01" @default.
• W2012193456 modified "2023-09-27" @default.
• W2012193456 title "Multifunctional enzymes and evolution of biosynthetic pathways: Retro-evolution by jumps" @default.
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• W2012193456 doi "https://doi.org/10.1002/(sici)1097-0134(19991101)37:2<303::aid-prot15>3.0.co;2-6" @default.
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