Literature DB >> 791073

Enzyme recruitment in evolution of new function.

R A Jensen.   

Abstract

Ancient cells must have possessed small gene content. Primitive enzymes may have possessed broad specificity and undeveloped regulation mechanisms. The considerable substrate ambiguity of these enzymes resulted in the formation of minor amounts of erroneous products. Fortuitous formation of metabolites offered ancient cells maximum biochemical flexibility with minimal gene content. Gene duplication provided the opportunity for increased gene content and increased specialization of the diverging enzymes, the substrate specialization being further reinforced by the development of regualtory mechanisms. Recuritment of enzymes for new pathways did not necessarily require the sequential and backwardly evolving progression of evolutionary steps required by the hypothesis of retrograde evolution of biochemical pathways. Substrate ambiguity remains a conspicuous feature of many contemporary proteins, and evolutionary exploitation of substrate ambiguity in a variety of organisms is still apparent.

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Year:  1976        PMID: 791073     DOI: 10.1146/annurev.mi.30.100176.002205

Source DB:  PubMed          Journal:  Annu Rev Microbiol        ISSN: 0066-4227            Impact factor:   15.500


  358 in total

1.  Functional prediction: identification of protein orthologs and paralogs.

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3.  Catalytic and binding poly-reactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution.

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4.  Prebiotic transamination.

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Journal:  J Mol Evol       Date:  1994-12       Impact factor: 2.395

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Journal:  J Mol Evol       Date:  2002-03       Impact factor: 2.395

7.  Functional versatility and molecular diversity of the metabolic map of Escherichia coli.

Authors:  S Tsoka; C A Ouzounis
Journal:  Genome Res       Date:  2001-09       Impact factor: 9.043

8.  The phylogenetic extent of metabolic enzymes and pathways.

Authors:  José Manuel Peregrin-Alvarez; Sophia Tsoka; Christos A Ouzounis
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9.  Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity.

Authors:  Andreas C Joerger; Sebastian Mayer; Alan R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  2003-04-23       Impact factor: 11.205

10.  The primordial metabolism: an ancestral interconnection between leucine, arginine, and lysine biosynthesis.

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