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Article

A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase.

Journal of molecular biology - 21 Mar 2008

Patrick Wayne M, Matsumura Ichiro

Abstract excerpt

The prevalence of paralogous enzymes implies that novel catalytic functions can evolve on preexisting protein scaffolds. The weak secondary activities of proteins, which reflect catalytic promiscuity and substrate ambiguity, are plausible starting points for this evolutionary process. In this study, we observed the emergence of a new enzyme from the ASKA (A Complete Set of E. coli K-12 ORF Archive) collection of...

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Share to Aldose-Ketose Isomerases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatography, High Pressure Liquid

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Share to Protein Structure, Tertiary

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Source

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Identifiers

PMID: 18272177
DOI: 10.1016/j.jmb.2008.01.043
PMCID: PMC2292674

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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