S-adenozilmetionin:tRNK riboziltransferaza-izomeraza

S-adenozilmetionin:tRNK riboziltransferaza-izomeraza
Identifikatori
EC broj2.4.99.17
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

S-adenozilmetionin:tRNK riboziltransferaza-izomeraza (EC 2.4.99.17, QueA enzim, kveozin biosinteza protein QueA) je enzim sa sistematskim imenom S-adenozil-L-metionin:7-aminometil-7-deazaguanozin riboziltransferaza (ribozil izomerizacija; L-metionin, otpuštanje adenina).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + 7-aminometil-7-karbaguanozin34 u tRNK L-metionin + adenin + epoksikveozin34 u tRNK

Ova reakcija je kombinovani transfer i izomerizacija ribozne grupe S-adenozil-L-metionina do modifikovanje guanozinske base u nestabilnoj poziciji tRNK molekula specifičnih za Tyr, His, Asp ili Asn.

Reference

  1. ^ Slany, R.K., Bosl, M., Crain, P.F. and 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: 7811—7817. PMID 8347586. 
  2. ^ Slany, R.K., Bosl, M. and 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: 389—393. PMID 7849103. 
  3. ^ Kinzie, S.D., Thern, B. and 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: 1307—1310. 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: 5312—5320. 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. and 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: 869—874. PMID 15822125. 
  6. ^ Grimm, C., Ficner, R., Sgraja, T., Haebel, P., Klebe, G. and Reuter, K. (2006). „Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase”. Biochem. Biophys. Res. Commun. 351: 695—701. PMID 17083917. 

Literatura

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