IscS Functions as a Primary Sulfur-donating Enzyme by Interacting Specifically with MoeB and MoaD in the Biosynthesis of Molybdopterin in Escherichia coli

The persulfide sulfur formed on an active site cysteine residue of pyridoxal 5′-phosphate-dependent cysteine desulfurases is subsequently incorporated into the biosynthetic pathways of a variety of sulfur-containing cofactors and thionucleosides. In molybdenum cofactor biosynthesis, MoeB activates t...

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Main Authors: Zhang, Wanjiao, Urban, Alexander, Mihara, Hisaaki, Leimkühler, Silke, Kurihara, Tatsuo, Esaki, Nobuyoshi
Formáid: Artigo
Teanga:Inglês
Foilsithe: American Society for Biochemistry and Molecular Biology 2010
Ábhair:
Enzyme Catalysis and Regulation
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2807287/
https://ncbi.nlm.nih.gov/pubmed/19946146
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.082172
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