EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
|---|
   2.4.99.17 | 718821 |
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 |
Escherichia coli |
8347586 |
| 2.4.99.17 | 718731 |
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase |
Biochem. Biophys. Res. Commun. |
351 |
695-701 |
2006 |
Bacillus subtilis |
17083917 |
| 2.4.99.17 | 721009 |
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 |
Thermotoga maritima |
15822125 |
| 2.4.99.17 | 718836 |
Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) |
Biochemistry |
42 |
5312-5320 |
2003 |
Escherichia coli |
12731872 |
| 2.4.99.17 | 720620 |
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 |
Escherichia coli |
10810734 |
| 2.4.99.17 | 719476 |
Structural analysis of the interaction of the tRNA modifying enzymes Tgt and QueA with a substrate tRNA |
FEBS Lett. |
361 |
259-264 |
1995 |
Escherichia coli |
7698334 |
| 2.4.99.17 | 719003 |
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 |
Escherichia coli |
7849103 |
| 2.4.99.17 | 719812 |
tRNA modification by S-adenosylmethionine:tRNA ribosyltransferase-isomerase. Assay development and characterization of the recombinant enzyme |
J. Biol. Chem. |
278 |
10491-10499 |
2003 |
Escherichia coli |
12533518 |
