Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.99 Transferring other glycosyl groups
ID:2.4.99.17
Description:S-adenosylmethionine:tRNA ribosyltransferase-isomerase.
Alternative Name: Queuosine biosynthesis protein QueA.
Cath: 2.40.10.240; 3.40.1780.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.99.17
BRENDA Enzyme Link: BRENDA 2.4.99.17
KEGG Enzyme Link: KEGG2.4.99.17
BioCyc Enzyme Link: BioCyc 2.4.99.17
ExPASy Enzyme Link: ExPASy2.4.99.17
EC2PDB Enzyme Link: EC2PDB 2.4.99.17
ExplorEnz Enzyme Link: ExplorEnz 2.4.99.17
PRIAM enzyme-specific profiles Link: PRIAM 2.4.99.17
IntEnz Enzyme Link: IntEnz 2.4.99.17
MEDLINE Enzyme Link: MEDLINE 2.4.99.17
MSA:

2.4.99.17;

Phylogenetic Tree:

2.4.99.17;

Uniprot:
M-CSA:
RHEA:32155 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-methionine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH2;+0:6]-[*:7]-[O;H0;+0:8]-[CH;+0:9](-[*:10])-[n;H0;+0:11](:[*:12]):[*:13]>>[*:1]-[NH;+0:2]-[CH;+0:9](-[*:10])-[CH;+0:6]1-[*:7]-[O;H0;+0:8]-1.[*:3]-[S;H0;+0:4]-[*:5].[*:12]:[nH;+0:11]:[*:13]
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References

TitleAuthorsDatePubMed ID
A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine.Slany RK, Bösl M, Crain PF, Kersten H1993 Aug 38347586
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.Slany RK, Bösl M, Kersten H19947849103
Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA).Van Lanen SG, Iwata-Reuyl D2003 May 1312731872
Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor.Kinzie SD, Thern B, Iwata-Reuyl D2000 May 410810734