Literature summary for 2.8.1.7 extracted from

Wu, G.; Li, P.; Wu, X.
Regulation of Escherichia coli IscS desulfurase activity by ferrous iron and cysteine (2008), Biochem. Biophys. Res. Commun., 374, 399-404.

Search for more literature for 2.8.1.7

Inhibitors

Inhibitors	Comment	Organism	Structure
Fe2+	the low desulfurase activity is caused by the modification of IscS rather than by the formation of FeS in the solution	Escherichia coli
additional information	desulfurase activity is gradually inhibited as the amount of iron and sulfide bound to IscS increases. When 2Fe-2S binds IscS, about 20% of the activity is inhibited, when 8Fe-8S adheres to IscS, about 70% of the activity is inhibited. Thus, the cell is able to modulate its desulfurase activity with the formation of an IscS-iron-sulfide complex	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	iron alone or iron together with sulfide binds to IscS to make IscS-iron or IscS-iron-sulfide complexes. The formation of such complexes allows the activity of IscS to be modulated effectively	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	recombinat enzyme	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-cysteine + ?	in the presence of cysteine, IscSs ability to bind iron improves significantly	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
cysteine desulfurase	-	Escherichia coli
IscS	-	Escherichia coli

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Release 2023.1 (January 2023)