1H, 15N, 13C backbone resonance assignments of human soluble catechol Omethyltransferase in complex with S-adenosyl-L-methionine and 3,5-dinitrocatechol

Research output: Contribution to journalArticle

  • External authors:
  • Sylwia Czarnota
  • Nicola Baxter
  • Matthew J Cliff
  • Jonathan Waltho

Abstract

Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT), found mostly in the brain. Here we report the backbone 1H, 15N and 13C chemical shift assignments of S-COMT in complex with S-adenosyl-L-methionine, 3,5-dinitrocatechol and Mg2+. Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97% of all backbone resonances were assigned in the complex, with 205 out of a possible 215 residues assigned in the 1H-15N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS+ webserver is in good agreement with published X-ray crystal structures.

Bibliographical metadata

Original languageEnglish
Pages (from-to)57-61
Number of pages5
JournalBiomolecular NMR Assignments
Volume11
Issue number1
Early online date15 Dec 2016
DOIs
StatePublished - Apr 2017