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EC Tree
IUBMB Comments The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, cysteine desulfurase, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
thiouridylase, mmp1354, rna sulfurtransferase, transfer rna sulfurtransferase,
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ribonucleate sulfurtransferase
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RNA sulfurtransferase
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transfer ribonucleate sulfurtransferase
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transfer RNA sulfurtransferase
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transferRNA thiolase
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ATP + [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-sulfur] cluster
on enzyme activation, an alpha-helix overhanging the active site is restructured into an idiosyncratic beta-hairpin-containing loop, which packs the flipped-out U34 deeply into the catalytic pocket and triggers the activation of the catalytic cysteine residues. The adenylated RNA intermediate is trapped. The active closed-conformation of the complex ensures accurate sulfur incorporation into the activated uridine carbon by forming a catalytic chamber to prevent solvent from accessing the catalytic site
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sulfur atom transfer
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[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine:uracil in tRNA sulfurtransferase
The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, cysteine desulfurase, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.
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L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
L-cysteine + E. coli 'activated' tRNA
L-serine + tRNA containing a thionucleotide
L-cysteine + poly A-2poly U
L-serine + S-tRNA
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L-cysteine + poly A-poly U
L-serine + S-tRNA
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L-cysteine + poly G,U
L-serine + S-tRNA
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G:U = 2
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L-cysteine + Saccharomyces cerevisiae 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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same activity with baker's yeast tRNA as RNA acceptor
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r
L-cysteine + tRNA
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additional information
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2-thiocytidine is the major thionucleotide formed in vitro, 4-thiouridine is the major product in vivo
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L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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r
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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r
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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sulfur deficient tRNA is the natural substrate
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r
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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enzyme is part of the sulfur-transferase system which forms 4-thiouridylate in tRNA
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r
L-cysteine + E. coli 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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Escherichia coli B tRNA and irradiated Escherichia coli tRNA, S-poor Escherichia coli tRNA also acts as RNA acceptors
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r
L-cysteine + E. coli 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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sulfur deficient tRNA is the natural substrate
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L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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sulfur deficient tRNA is the natural substrate
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r
L-cysteine + 'activated' tRNA
L-serine + tRNA containing a thionucleotide
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enzyme is part of the sulfur-transferase system which forms 4-thiouridylate in tRNA
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r
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additional information
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beta-mercaptopyruvate is inactive either as a cofactor or as a sulfur donor
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Cd2+
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inhibits the synthesis of s4U
Co2+
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inhibits the synthesis of s4U
Fe2+
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inhibits the synthesis of s4U
Ni2+
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inhibits the synthesis of s4U
Zn2+
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inhibits the synthesis of s4U
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0.0027
tRNA
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pH 7.5, 37°C, sulfur deficient tRNA
0.0012 - 0.0016
L-cysteine
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pH 7.8, 37°C
0.26
L-cysteine
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pH 7.5, 37°C
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UniProt
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-20°C, partly purified pooled protein fractions can be stored indefinitely for periods up to several months
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4°C, addition of toluene, can be stored indefinitely for periods up to several months
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sulfurtransferase system with 2 enzymes
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Abrell, J.W.; Kaufman, E.E.; Lipsett, M.N.
The biosynthesis of 4-thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system
J. Biol. Chem.
246
294-301
1971
Escherichia coli, Escherichia coli B / ATCC 11303
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Harris, C.L.; Titchener, E.B.
Sulfur-deficient transfer ribonucleic acid. The natural substrate for ribonucleic acid sulfurtransferase from Escherichia coli
Biochemistry
10
4207-4212
1971
Escherichia coli, Escherichia coli HfrC
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Numata, T.; Ikeuchi, Y.; Fukai, S.; Suzuki, T.; Nureki, O.
Snapshots of tRNA sulphuration via an adenylated intermediate
Nature
442
419-424
2006
Escherichia coli (P25745)
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