The self-inhibitory nature of metabolic networks and its alleviation through compartmentalization View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-07-10

AUTHORS

Mohammad Tauqeer Alam, Viridiana Olin-Sandoval, Anna Stincone, Markus A. Keller, Aleksej Zelezniak, Ben F. Luisi, Markus Ralser

ABSTRACT

Metabolites can inhibit the enzymes that generate them. To explore the general nature of metabolic self-inhibition, we surveyed enzymological data accrued from a century of experimentation and generated a genome-scale enzyme-inhibition network. Enzyme inhibition is often driven by essential metabolites, affects the majority of biochemical processes, and is executed by a structured network whose topological organization is reflecting chemical similarities that exist between metabolites. Most inhibitory interactions are competitive, emerge in the close neighbourhood of the inhibited enzymes, and result from structural similarities between substrate and inhibitors. Structural constraints also explain one-third of allosteric inhibitors, a finding rationalized by crystallographic analysis of allosterically inhibited L-lactate dehydrogenase. Our findings suggest that the primary cause of metabolic enzyme inhibition is not the evolution of regulatory metabolite-enzyme interactions, but a finite structural diversity prevalent within the metabolome. In eukaryotes, compartmentalization minimizes inevitable enzyme inhibition and alleviates constraints that self-inhibition places on metabolism. More... »

PAGES

16018

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms16018

DOI

http://dx.doi.org/10.1038/ncomms16018

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1090574504

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28691704


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