Structural highlights
Function
CNTA_ACIB2 Converts carnitine to trimethylamine and malic semialdehyde.[HAMAP-Rule:MF_02097][1]
Publication Abstract from PubMed
Rieske monooxygenases undertake complex catalysis integral to marine, terrestrial and human gut-ecosystems. Group-I to IV Rieske monooxygenases accept aromatic substrates and have well characterised catalytic mechanisms. Nascent to our understanding are Group-V members catalysing the oxidation/breakdown of quaternary ammonium substrates. Phylogenetic analysis of Group V highlights a cysteine residue-pair adjacent to the mononuclear Fe active site with no established role. Following our elucidation of the carnitine monooxygenase CntA structure, we probed the function of the cysteine pair Cys206/Cys209. Utilising biochemical and biophysical techniques, we found the cysteine residues do not play a structural role nor influence the electron transfer pathway, but rather are used in a non-stoichiometric role to ensure the catalytic iron centre remains in an Fe(II) state.
Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site.,Quareshy M, Shanmugam M, Cameron AD, Bugg TDH, Chen Y FEBS J. 2023 Jan 8. doi: 10.1111/febs.16722. PMID:36617384[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhu Y, Jameson E, Crosatti M, Schafer H, Rajakumar K, Bugg TD, Chen Y. Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota. Proc Natl Acad Sci U S A. 2014 Mar 18;111(11):4268-73. doi: , 10.1073/pnas.1316569111. Epub 2014 Mar 3. PMID:24591617 doi:http://dx.doi.org/10.1073/pnas.1316569111
- ↑ Quareshy M, Shanmugam M, Cameron AD, Bugg TDH, Chen Y. Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site. FEBS J. 2023 Jan 8. doi: 10.1111/febs.16722. PMID:36617384 doi:http://dx.doi.org/10.1111/febs.16722
