EC 2.4.99.17 - S-adenosylmethionine:tRNA ribosyltransferase-isomerase

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IntEnz Enzyme Nomenclature
EC 2.4.99.17

Names

Accepted name:
S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Other names:
QueA enzyme
queuosine biosynthesis protein QueA
Systematic name:
S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing L-methionine, adenine releasing)

Reaction

Comments:

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. It is part of the queuosine biosynthesis pathway.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (536) [show] [UniProt]

References

  1. Slany, R. K., Bosl, M., Crain, P. F., Kersten, H.
    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: 7811-7817 (1993). [PMID: 8347586]
  2. Slany, R. K., Bosl, M., Kersten, H.
    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: 389-393 (1994). [PMID: 7849103]
  3. Kinzie, S. D., Thern, B., Iwata-Reuyl, D.
    Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor.
    Org. Lett. 2: 1307-1310 (2000). [PMID: 10810734]
  4. Van Lanen, S. G., Iwata-Reuyl, D.
    Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA).
    Biochemistry 42: 5312-5320 (2003). [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.
    Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold.
    Proteins 59: 869-874 (2005). [PMID: 15822125]
  6. Grimm, C., Ficner, R., Sgraja, T., Haebel, P., Klebe, G., Reuter, K.
    Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase.
    Biochem. Biophys. Res. Commun. 351: 695-701 (2006). [PMID: 17083917]

[EC 2.4.99.17 created 2012]