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Literature summary for 2.3.1.234 extracted from

  • Lauhon, C.T.
    Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP (2012), Biochemistry, 51, 8950-8963.
    View publication on PubMed
Search for more literature for 2.3.1.234

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O05518
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-
Bacillus subtilis 168 O05518
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonylcarbamoyladenylate + adenine37 in tRNA
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 Bacillus subtilis AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
 ?
L-threonylcarbamoyladenylate + adenine37 in tRNA
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 Bacillus subtilis 168 AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
 ?

Synonyms

Synonyms Comment Organism
TsaD
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 Bacillus subtilis
YdiE
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 Bacillus subtilis

General Information

General Information Comment Organism
physiological function N6-threonylcarbamoyladenonsine biosynthesis in Bacillus subtilis requires the four proteins Ywl/TsaC, YdiB/TsaE, YdiC/TsaB and YdiE/TsaD. YwlC catalyzes the conversion of L-threonine, bicarbonate/CO2 and ATP to give the intermediate L-threonylcarbamoyl-AMP and diphosphate as products. Purified L-threonylcarbamoyl-AMP is efficiently processed to N6-threonylcarbamoyladenonsine by the YdiBCE proteins in the presence of tRNA substrates. This reaction is ATP independent in vitro. Data suggest channeling of the intermediate Bacillus subtilis