Abstract
A core of widely distributed network branches biosynthesizing at least 16 out of the 20 standard amino acids is predicted using comparative genomics.
Highlights
Twenty amino acids comprise the universal building blocks of proteins
Biological distribution of amino acid biosynthetic networks The origins and evolution of amino acid biosynthesis were assessed by analyzing the taxonomic distributions (TDs) of its catalyzing enzymes
The rationale is that TDs provide clues concerning the relative appearance of enzymes, branches and pathways during the evolution of metabolism
Summary
Twenty amino acids comprise the universal building blocks of proteins Their biosynthetic routes do not appear to be universal from an Escherichia coli-centric perspective. We use a comparative genomics approach to assess the origins and evolution of alternative amino acid biosynthetic network branches. It is likely that a small number of enzymes with broad specificity existed in early stages of metabolic evolution. Genes encoding these enzymes probably have been duplicated, generating paralog enzymes that, through sequence divergence, became more specialized, giving rise, for instance, to the isomerases HisA (EC:5.3.1.16) and TrpC (EC:5.3.1.24), which act in histidine and tryptophan biosynthesis, respectively [1,2,3,4]. The new perspective views metabolic components (substrates, products, cofactors, and enzymes) as nodes forming branches within a single network [5,6]
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