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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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| Main Authors: | , , , , , |
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| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
American Society for Biochemistry and Molecular Biology
2011
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| Ábhair: | |
| Rochtain Ar Líne: | 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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