S-adenozilmetionin:tRNA ribosyltransferase-isomerase

S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Identifiers
EC number 2.4.99.17
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

S-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 2.4.99.17, QueA enzyme, queuosine biosynthesis protein QueA) is an enzyme with systematic name S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine34 in tRNA L-methionine + adenine + epoxyqueuosine34 in tRNA

The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn.

References

  1. ↑ Slany, R.K.; Bosl, M.; Crain, P.F.; Kersten, H. (1993). "A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine". Biochemistry. 32 (30): 7811–7817. doi:10.1021/bi00081a028. PMID 8347586.
  2. ↑ Slany, R.K.; Bosl, M.; Kersten, H. (1994). "Transfer and isomerization of the ribose moiety of AdoMet during the biosynthesis of queuosine tRNAs, a new unique reaction catalyzed by the QueA protein from Escherichia coli". Biochimie. 76 (5): 389–393. doi:10.1016/0300-9084(94)90113-9. PMID 7849103.
  3. ↑ Kinzie, S.D.; Thern, B.; Iwata-Reuyl, D. (2000). "Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor". Org. Lett. 2 (9): 1307–1310. doi:10.1021/ol005756h. PMID 10810734.
  4. ↑ Van Lanen, S.G.; Iwata-Reuyl, D. (2003). "Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)". Biochemistry. 42 (18): 5312–5320. doi:10.1021/bi034197u. PMID 12731872.
  5. ↑ Mathews, I.; Schwarzenbacher, R.; McMullan, D.; Abdubek, P.; Ambing, E.; Axelrod, H.; Biorac, T.; Canaves, J.M.; Chiu, H.J.; Deacon, A.M.; DiDonato, M.; Elsliger, M.A.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Hale, J.; Hampton, E.; Han, G.W.; Haugen, J.; Hornsby, M.; Jaroszewski, L.; Klock, H.E.; Koesema, E.; Kreusch, A.; Kuhn, P.; Lesley, S.A.; Levin, I.; Miller, M.D.; Moy, K.; Nigoghossian, E.; Ouyang, J.; Paulsen, J.; Quijano, K.; Reyes, R.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Velasquez, J.; Vincent, J.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Wilson, I.A. (2005). "Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold". Proteins. 59 (4): 869–874. doi:10.1002/prot.20419. PMID 15822125.
  6. ↑ Grimm, C.; Ficner, R.; Sgraja, T.; Haebel, P.; Klebe, G.; Reuter, K. (2006). "Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase". Biochem. Biophys. Res. Commun. 351 (3): 695–701. doi:10.1016/j.bbrc.2006.10.096. PMID 17083917.
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