Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ikeuchi, Y.; Shigi, N.; Kato, J.; Nishimura, A.; Suzuki, T.
    Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. (2006), Mol. Cell, 21, 97-108.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.13 TusE-SSH + adenylated-tRNA-uridine Escherichia coli the wobble bases of bacterial tRNAs responsible for NNR codons are modified to 5-methylaminomethyl-2-thiouridine (mnm5s2U). 2-thio modification of mnm5s2U is required for accurate decoding and essential for normal cell growth. IscS and MnmA are the minimum essential factors for 2-thiolation of mnm5s2U in vitro. TusE directly interacts with MnmA-tRNA to form a ternary complex. TusE appears to interact with MnmA, but not with tRNA, because TusE-tRNA interactions are not observed TusE-SH + tRNA-2-thiouridine + AMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.13 Escherichia coli P25745
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.13 TusE-SSH + adenylated-tRNA-uridine the wobble bases of bacterial tRNAs responsible for NNR codons are modified to 5-methylaminomethyl-2-thiouridine (mnm5s2U). 2-thio modification of mnm5s2U is required for accurate decoding and essential for normal cell growth. IscS and MnmA are the minimum essential factors for 2-thiolation of mnm5s2U in vitro. TusE directly interacts with MnmA-tRNA to form a ternary complex. TusE appears to interact with MnmA, but not with tRNA, because TusE-tRNA interactions are not observed Escherichia coli TusE-SH + tRNA-2-thiouridine + AMP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.8.1.13 MnmA
-
 Escherichia coli