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Literature summary for 2.8.1.B3 extracted from

  • Lauhon, C.; Erwin, W.; Ton, G.
    Substrate specificity for 4-thiouridine modification in Escherichia coli (2004), J. Biol. Chem., 279, 23022-23029.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Sulfide optimal sulfide concentration for 4-thiouridine modification of tRNAPhe is about 50 mM. Higher sulfide concentrations are inhibitory Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8) Escherichia coli the biosynthesis of 4-thiouridine in Escherichia coli tRNA requires the action of both the thiamine pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from L-cysteine to ThiI, which utilizes MgATP2- to activate uridine 8 in tRNA and transfers sulfur to give s4U sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfide + adenylated-tRNA-uridine(position8) sulfide is able to replace IscS/cysteine as a substrate for 4-thiouridine synthesis Escherichia coli tRNA-4-thiouridine(position8) + ?
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sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8) the biosynthesis of 4-thiouridine in Escherichia coli tRNA requires the action of both the thiamine pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from L-cysteine to ThiI, which utilizes MgATP2- to activate uridine 8 in tRNA and transfers sulfur to give s4U Escherichia coli sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
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sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8) the biosynthesis of 4-thiouridine in Escherichia coli tRNA requires the action of both the thiamin pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from L-cysteine to ThiI, which utilizes MgATP2- to activate uridine 8 in tRNA and transfers sulfur to give s4U. Outside of the modified uridine 8, there is no primary sequence requirement for substrate recognition. However, the secondary and tertiary structure restrictions appear sufficient to explain why s4U modification is limited in the cell to tRNA Escherichia coli sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
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