IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli.

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  • Author(s): Zhang W;Zhang W; Urban A; Mihara H; Leimkühler S; Kurihara T; Esaki N
  • Source:
    The Journal of biological chemistry [J Biol Chem] 2010 Jan 22; Vol. 285 (4), pp. 2302-8. Date of Electronic Publication: 2009 Nov 29.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Carbon-Sulfur Lyases/*metabolism ; Coenzymes/*biosynthesis ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*metabolism ; Metalloproteins/*biosynthesis ; Nucleotidyltransferases/*metabolism ; Sulfurtransferases/*metabolism; Carbon-Sulfur Lyases/chemistry ; Catalytic Domain ; Cysteine/metabolism ; Escherichia coli Proteins/chemistry ; Molybdenum Cofactors ; Nucleotidyltransferases/chemistry ; Protein Binding ; Pteridines ; Species Specificity ; Sulfur/metabolism ; Sulfur Compounds/metabolism ; Sulfurtransferases/chemistry ; Surface Plasmon Resonance
    • Abstract:
      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 the C terminus of the MoaD subunit of molybdopterin (MPT) synthase to form MoaD-adenylate, which is subsequently converted to a thiocarboxylate for the generation of the dithiolene group of MPT. It has been shown that three cysteine desulfurases (CsdA, SufS, and IscS) of Escherichia coli can transfer sulfur from l-cysteine to the thiocarboxylate of MoaD in vitro. Here, we demonstrate by surface plasmon resonance analyses that IscS, but not CsdA or SufS, interacts with MoeB and MoaD. MoeB and MoaD can stimulate the IscS activity up to 1.6-fold. Analysis of the sulfuration level of MoaD isolated from strains defective in cysteine desulfurases shows a largely decreased sulfuration level of the protein in an iscS deletion strain but not in a csdA/sufS deletion strain. We also show that another iscS deletion strain of E. coli accumulates compound Z, a direct oxidation product of the immediate precursor of MPT, to the same extent as an MPT synthase-deficient strain. In contrast, analysis of the content of compound Z in DeltacsdA and DeltasufS strains revealed no such accumulation. These findings indicate that IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of MPT synthase in MPT biosynthesis.
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    • Accession Number:
      0 (Coenzymes)
      0 (Escherichia coli Proteins)
      0 (Metalloproteins)
      0 (Molybdenum Cofactors)
      0 (Pteridines)
      0 (Sulfur Compounds)
      70FD1KFU70 (Sulfur)
      ATN6EG42UQ (molybdenum cofactor)
      EC 2.7.7.- (MoeB protein, E coli)
      EC 2.7.7.- (Nucleotidyltransferases)
      EC 2.8.1.- (Sulfurtransferases)
      EC 2.8.1.- (molybdopterin synthase)
      EC 4.4.- (Carbon-Sulfur Lyases)
      EC 4.4.1.- (cysteine desulfurase)
      K848JZ4886 (Cysteine)
    • Publication Date:
      Date Created: 20091201 Date Completed: 20100222 Latest Revision: 20211203
    • Publication Date:
      20240829
    • Accession Number:
      PMC2807287
    • Accession Number:
      10.1074/jbc.M109.082172
    • Accession Number:
      19946146