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. Author manuscript; available in PMC: 2009 Jan 1.
Published in final edited form as: Prog Lipid Res. 2007 Nov 1;47(1):50–61. doi: 10.1016/j.plipres.2007.10.002

Fig. 13.

Fig. 13

Representation of the S (left) and the R (right) enantiomers of the CoA of the 2-OMe:14:0 inside the active site of a partial model of the enzyme Sc-NMT. The methoxy oxygen of the S-enantiomer hydrogen bonds to a Threonine 205 (left). (Picture courtesy of Prof. Amiram Goldblum, Hebrew University of Jerusalem).