Biology:S-Adenozilmetionin:tRNA ribosyltransferase-isomerase
From HandWiki
Short description: Class of enzymes
| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "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): 7811–7. August 1993. doi:10.1021/bi00081a028. PMID 8347586.
- ↑ "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): 389–93. 1994. doi:10.1016/0300-9084(94)90113-9. PMID 7849103.
- ↑ "Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor". Organic Letters 2 (9): 1307–10. May 2000. doi:10.1021/ol005756h. PMID 10810734.
- ↑ "Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)". Biochemistry 42 (18): 5312–20. May 2003. doi:10.1021/bi034197u. PMID 12731872.
- ↑ "Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold". Proteins 59 (4): 869–74. June 2005. doi:10.1002/prot.20419. PMID 15822125.
- ↑ "Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase". Biochemical and Biophysical Research Communications 351 (3): 695–701. December 2006. doi:10.1016/j.bbrc.2006.10.096. PMID 17083917.
External links
- S-adenosylmethionine:tRNA+ribosyltransferase-isomerase at the US National Library of Medicine Medical Subject Headings (MeSH)
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