Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation - PubMed (original) (raw)

. 2016 Aug 26;55(36):10630-3.

doi: 10.1002/anie.201603882. Epub 2016 Jul 28.

Affiliations

• PMID: 27467699
• DOI: 10.1002/anie.201603882

Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation

Tristan Wagner et al. Angew Chem Int Ed Engl. 2016.

Abstract

All methanogenic and methanotrophic archaea known to date contain methyl-coenzyme M reductase (MCR) that catalyzes the reversible reduction of methyl-coenzyme M to methane. This enzyme contains the nickel porphinoid F430 as a prosthetic group and, highly conserved, a thioglycine and four methylated amino acid residues near the active site. We describe herein the presence of a novel post-translationally modified amino acid, didehydroaspartate, adjacent to the thioglycine as revealed by mass spectrometry and high-resolution X-ray crystallography. Upon chemical reduction, the didehydroaspartate residue was converted into aspartate. Didehydroaspartate was found in MCR I and II from Methanothermobacter marburgensis and in MCR of phylogenetically distantly related Methanosarcina barkeri but not in MCR I and II of Methanothermobacter wolfeii, which indicates that didehydroaspartate is dispensable but might have a role in fine-tuning the active site to increase the catalytic efficiency.

Keywords: didehydroaspartate; enzyme catalysis; methyl-coenzyme M reductase; post-translational modification.

© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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