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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: | , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Biochemistry and Molecular Biology
2010
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| Fag: | |
| Online adgang: | 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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