EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  2.8.1.13 | a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor |
- |
Bacillus subtilis |
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor |
enzyme adenylates and subsequently thiolates tRNA to form the s2U modification |
? |
| 2.8.1.13 | a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor |
the enzyme functions on tRNALys(mnm5s2UUU), tRNAGlu(mnm5s2UUC), and tRNAGln((c)mnm5s2UUG) |
Escherichia coli |
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor |
- |
? |
| 2.8.1.13 | a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor |
- |
Bacillus subtilis 168 |
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor |
enzyme adenylates and subsequently thiolates tRNA to form the s2U modification |
? |
| 2.8.1.13 | more |
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance |
Escherichia coli |
? |
- |
? |
| 2.8.1.13 | more |
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. Purified IscS-persulfide is able to provide sulfur for in vitro s2U synthesis in the absence of cysteine. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance. Identification of 2-thiouridine as product of the in vitro s2U reaction. |
Escherichia coli |
? |
- |
? |
| 2.8.1.13 | more |
in the IscSeMnmA pathway, protein MnmA, together with the cysteine desulfurase IscS and sulfur transfer mediators TusA-E, performs thiolation at position 2 of U34, which occurs only in tRNALys mnm5s2UUU, tRNAGlu mnm5s2UUC, tRNAGln cmnm5s2UUG |
Escherichia coli |
? |
- |
? |
| 2.8.1.13 | TusE-SSH + adenylated-tRNA-uridine |
- |
Escherichia coli |
TusE-SH + tRNA-2-thiouridine + AMP |
- |
? |
| 2.8.1.13 | TusE-SSH + adenylated-tRNA-uridine |
MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNAGlu, tRNAGln and tRNALys in Escherichia coli |
Escherichia coli |
TusE-SH + tRNA-2-thiouridine + AMP |
- |
? |
| 2.8.1.13 | TusE-SSH + adenylated-tRNA-uridine |
the biogenesis of 2-thiouridine in Escherichia coli utilizes persulfide chemistry and proceeds through a complex sulfur-relay system by multiple sulfur mediators that select and facilitate specific sulfur flow to 2-thiouridine from various cellular sulfur pathways. TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP |
Escherichia coli |
TusE-SH + tRNA-2-thiouridine + AMP |
- |
? |
| 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 |
- |
? |
