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Title: Structure of aryl O -demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [1];  [2];  [3];  [1]
  1. Joint BioEnergy Institute, Emeryville, CA 94608,, Biomass Science and Conversion Technology Department, Sandia National Laboratories, Livermore, CA 94550,
  2. Joint BioEnergy Institute, Emeryville, CA 94608,, Biosciences Area, Lawrence Berkeley National Laboratory, Berkeley, CA 94720,, Department of Bioengineering, University of California, Berkeley, CA 94720
  3. Joint BioEnergy Institute, Emeryville, CA 94608,, Biosciences Area, Lawrence Berkeley National Laboratory, Berkeley, CA 94720,
+ Show Author Affiliations

Significance Modern industrial and agricultural practices generate large quantities of aromatic pollutants; however, these waste products can be converted into fine chemicals, fuels, and plastics through biocatalytic pathways. The bacterial world can inform such utilization strategies as certain strains of soil and marine bacteria metabolize environmentally derived aromatics. Many of these metabolic pathways involve aryl intermediates that require demethylation to facilitate modification and ring opening for assimilation into the tricarboxylic acid (TCA) cycle. Aryl demethylases, which catalyze this reaction, are poorly understood, making their utilization in biotechnology difficult. We provide the structural and mechanistic characterization of a single-domain aryl demethylase, LigM, which employs a tyrosine-dependent mechanism. Insights from this work will inform synthetic biology approaches to convert underutilized aromatics into higher value compounds.

Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1349696
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 16 Vol. 114; ISSN 0027-8424
Publisher:
Proceedings of the National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
English

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