Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-10

AUTHORS

D J Neidhart, G L Kenyon, J A Gerlt, G A Petsko

ABSTRACT

Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) catalyse separate and mechanistically distinct reactions necessary for the catabolism of aromatic acids by Pseudomonas putida. The X-ray crystal structure of MR, solved at 2.5 A resolution, reveals that the secondary, tertiary and quaternary structures of MR and MLE are remarkably similar; also, MR and MLE are about 26% identical in primary structure. However, MR has no detectable MLE activity and vice versa. Thus, MR and MLE constitute the first example of enzymes that catalyse different reactions, as opposed to mechanistically identical reactions on different substrates, yet possess sufficient structural and sequence identity that they are likely to have evolved from a common ancestor. The discovery that MR and MLE catalyse different reactions but share a common structural framework has broad implications for the natural evolution of enzymes and metabolic pathways, as well as for the rational modification of enzyme activities. More... »

PAGES

692-694

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

6294

VOLUME

347

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/347692a0

    DOI

    http://dx.doi.org/10.1038/347692a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1052260843

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/2215699


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