S-Adenosyl-S-carboxymethyl-l-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA

Byrne, R.T.; Whelan, F.; Aller, P.; Bird, L.E.; Dowle, A.; Lobley, C.M.C.; Reddivari, Y.; Nettleship, J.E.; Owens, R.J.; Antson, A.A.; Waterman, D.G.

doi:10.1107/S0907444913004939

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
The proposed modification pathway of 5-oxyuridine derivatives. CmoA has been implicated in the modification of mo⁵U to cmo⁵U (Nasvall et al., 2004

), although this reaction involves more than the addition of a single methyl group, indicating that either additional enzymes and/or cofactors are involved. No enzymes involved in the conversion of U to ho⁵U or cmo⁵U to mcmo⁵U have been identified.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 69| Part 6| June 2013| Pages 1090-1098

https://doi.org/10.1107/S0907444913004939

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