Crystal Structure of the Heme d(1) Biosynthesis Enzyme NirE in Complex with Its Substrate Reveals New Insights into the Catalytic Mechanism of S-Adenosyl-l-methionine-dependent Uroporphyrinogen III Methyltransferases

During the biosynthesis of heme d(1), the essential cofactor of cytochrome cd(1) nitrite reductase, the NirE protein catalyzes the methylation of uroporphyrinogen III to precorrin-2 using S-adenosyl-l-methionine (SAM) as the methyl group donor. The crystal structure of Pseudomonas aeruginosa NirE in...

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Detalhes bibliográficos
Main Authors: Storbeck, Sonja, Saha, Sayantan, Krausze, Joern, Klink, Björn U., Heinz, Dirk W., Layer, Gunhild
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2011
Assuntos:
Protein Structure and Folding
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3143637/
https://ncbi.nlm.nih.gov/pubmed/21632530
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.239855
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