Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

hemN - coproporphyrinogen III oxidase

Escherichia coli UTI89

Layer, G. et al., Layer, G. et al., Layer, G. et al., Layer, G. et al.

Layer, Pierik, Trost, Rigby, Leech, Grage, Breckau, Astner, Jänsch, Heathcote, Warren, Heinz, Jahn,

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Disease relevance of hemN

We present the first crystal structure of a Radical SAM enzyme, that of HemN, the Escherichia coli oxygen-independent coproporphyrinogen III oxidase, at 2.07 A resolution [1].

High impact information on hemN

During porphyrin biosynthesis the oxygen-independent coproporphyrinogen III oxidase (HemN) catalyzes the oxidative decarboxylation of the propionate side chains of rings A and B of coproporphyrinogen III to form protoporphyrinogen IX [2].
In this review, we report the characterization of two enzymes: the established radical SAM enzyme, HemN or oxygen-independent coproporphyrinogen III oxidase from Escherichia coli, and littorine mutase, a presumed radical SAM enzyme, responsible for the conversion of littorine to hyoscyamine in plants [3].

Associations of hemN with chemical compounds

The S-adenosylmethionine (AdoMet) radical enzyme oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX during bacterial heme biosynthesis [4].

References

Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes. Layer, G., Moser, J., Heinz, D.W., Jahn, D., Schubert, W.D. EMBO J. (2003) [Pubmed]
The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN. Layer, G., Pierik, A.J., Trost, M., Rigby, S.E., Leech, H.K., Grage, K., Breckau, D., Astner, I., Jänsch, L., Heathcote, P., Warren, M.J., Heinz, D.W., Jahn, D. J. Biol. Chem. (2006) [Pubmed]
Structural and functional comparison of HemN to other radical SAM enzymes. Layer, G., Kervio, E., Morlock, G., Heinz, D.W., Jahn, D., Retey, J., Schubert, W.D. Biol. Chem. (2005) [Pubmed]
Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines. Layer, G., Grage, K., Teschner, T., Schünemann, V., Breckau, D., Masoumi, A., Jahn, M., Heathcote, P., Trautwein, A.X., Jahn, D. J. Biol. Chem. (2005) [Pubmed]

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