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Literature summary for 2.8.1.7 extracted from

  • Neumann, M.; Stoecklein, W.; Walburger, A.; Magalon, A.; Leimkuehler, S.
    Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase (2007), Biochemistry, 46, 9586-9595.
    View publication on PubMed
Search for more literature for 2.8.1.7

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rhodobacter capsulatus enzyme NifS4 is involved in formation of the Mo-S ligand of Moco. It mobilizes sulfur by formation of a protein-bound persulfide intermediate and transfers this sulfur further to Moco. Moco is sulfurated before the insertion into xanthine dehydrogenase, while it is bound to XdhC ?
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 ?
additional information Rhodobacter capsulatus NifS4 is involved in the formation of the Mo=S ligand of molybdenum cofactor. NifS4 mobilizes sulfur from L-cysteine by formation of a protein-bound persulfide intermediate and transfers this sulfur further to molybdenum cofactor. Molybdenum cofactor is sulfurated before the insertion into XDH, while it is bound to XdhC ?
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 ?

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
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-
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Rhodobacter capsulatus
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 expression in Escherichia coli BL21(DE3)
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Reaction

Reaction Comment Organism Reaction ID
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor enzyme NifS4 is involved in formation of the Mo-S ligand of Moco. It mobilizes sulfur by formation of a protein-bound persulfide intermediate and transfers this sulfur further to Moco. Moco is sulfurated before the insertion into xanthine dehydrogenase, while it is bound to XdhC Rhodobacter capsulatus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme NifS4 is involved in formation of the Mo-S ligand of Moco. It mobilizes sulfur by formation of a protein-bound persulfide intermediate and transfers this sulfur further to Moco. Moco is sulfurated before the insertion into xanthine dehydrogenase, while it is bound to XdhC Rhodobacter capsulatus ?
-
 ?
additional information NifS4 is involved in the formation of the Mo=S ligand of molybdenum cofactor. NifS4 mobilizes sulfur from L-cysteine by formation of a protein-bound persulfide intermediate and transfers this sulfur further to molybdenum cofactor. Molybdenum cofactor is sulfurated before the insertion into XDH, while it is bound to XdhC Rhodobacter capsulatus ?
-
 ?

Subunits

Subunits Comment Organism
More cysteine desulfurase NifS4 interacts with XdhC, but not with xanthine dehydrogenase Rhodobacter capsulatus

Synonyms

Synonyms Comment Organism
L-cysteine desulfurase
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 Rhodobacter capsulatus
NifS4
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 Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
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 Rhodobacter capsulatus