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词条 S-adenozilmetionin:tRNA ribosyltransferase-isomerase
释义

  1. References

  2. External links

{{Infobox enzyme
| Name = S-adenosylmethionine:tRNA ribosyltransferase-isomerase
| EC_number = 2.4.99.17
| CAS_number =
| IUBMB_EC_number = 2/4/99/17
| GO_code =
| image =
| width =
| caption =
}}S-adenosylmethionine:tRNA ribosyltransferase-isomerase ({{EC number|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. ^{{cite journal | vauthors = Slany RK, Bösl M, Crain PF, Kersten H | title = A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine | journal = Biochemistry | volume = 32 | issue = 30 | pages = 7811–7 | date = August 1993 | pmid = 8347586 | doi = 10.1021/bi00081a028 }}
2. ^{{cite journal | vauthors = Slany RK, Bösl M, Kersten H | title = 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 | journal = Biochimie | volume = 76 | issue = 5 | pages = 389–93 | year = 1994 | pmid = 7849103 | doi = 10.1016/0300-9084(94)90113-9 }}
3. ^{{cite journal | vauthors = Kinzie SD, Thern B, Iwata-Reuyl D | title = Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor | journal = Organic Letters | volume = 2 | issue = 9 | pages = 1307–10 | date = May 2000 | pmid = 10810734 | doi = 10.1021/ol005756h }}
4. ^{{cite journal | vauthors = Van Lanen SG, Iwata-Reuyl D | title = Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) | journal = Biochemistry | volume = 42 | issue = 18 | pages = 5312–20 | date = May 2003 | pmid = 12731872 | doi = 10.1021/bi034197u }}
5. ^{{cite journal | vauthors = Mathews I, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Miller MD, Moy K, Nigoghossian E, Ouyang J, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA | display-authors = 6 | title = Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold | journal = Proteins | volume = 59 | issue = 4 | pages = 869–74 | date = June 2005 | pmid = 15822125 | doi = 10.1002/prot.20419 }}
6. ^{{cite journal | vauthors = Grimm C, Ficner R, Sgraja T, Haebel P, Klebe G, Reuter K | title = Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase | journal = Biochemical and Biophysical Research Communications | volume = 351 | issue = 3 | pages = 695–701 | date = December 2006 | pmid = 17083917 | doi = 10.1016/j.bbrc.2006.10.096 }}

External links

  • {{MeshName|S-adenosylmethionine:tRNA+ribosyltransferase-isomerase}}
{{Glycosyltransferases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}

1 : EC 2.4.99

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