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Literature summary for 2.8.1.7 extracted from

  • Zhang, W.; Urban, A.; Mihara, H.; Leimkuehler, S.; Kurihara, T.; Esaki, N.
    IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli (2010), J. Biol. Chem., 285, 2302-2308.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.8.1.7

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Toyopearl column chromatography and phenyl-Toyopearl column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + [enzyme]-cysteine IscS transfers the sulfur atom from L-cysteine to the C-terminal thiocarboxylate of the MoaD subunit in vitro Escherichia coli L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
additional information IscS is involved in the sulfuration of MoaD subunit Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
IscS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli the IscS activity is stimulated up to 1.6fold in the presence of 10fold molar excess of MoeB subunit, the addition of MoaD subunit to a mixture of IscS and MoeB subunit detectably enhances the desulfurase activity to levels much higher than those observed for the addition of MoeB subunit alone to IscS up

General Information

General Information Comment Organism
physiological function IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of molybdopterin synthase in molybdopterin biosynthesis Escherichia coli