EC number:2.8.4.3
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.8 Transferring sulfur-containing groups |
| 2.8.4 Transferring alkylthio groups |
| ID: | 2.8.4.3 |
|---|---|
| Description: | tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase. |
| Alternative Name: |
tRNA-i6A37 methylthiotransferase. 2-methylthio-N-6-isopentenyl adenosine synthase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.8.4.3 |
| BRENDA Enzyme Link: | BRENDA 2.8.4.3 |
| KEGG Enzyme Link: | KEGG2.8.4.3 |
| BioCyc Enzyme Link: | BioCyc 2.8.4.3 |
| ExPASy Enzyme Link: | ExPASy2.8.4.3 |
| EC2PDB Enzyme Link: | EC2PDB 2.8.4.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.8.4.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.8.4.3 |
| IntEnz Enzyme Link: | IntEnz 2.8.4.3 |
| MEDLINE Enzyme Link: | MEDLINE 2.8.4.3 |
| RHEA:37067 | [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*;H0;+0:1]-[SH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH2;+0:6]-[*:7].[*:8]-[S+;H0:9](-[*:10])-[CH3;+0:11].[*:12]:[cH;+0:13]:[*:14]>>[*;H0;+0:1].[*:7]-[CH3;+0:6].[*:8]-[S;H0;+0:9]-[*:10].[*:3]-[S;H0;+0:4]-[*:5].[*:12]:[c;H0;+0:13](:[*:14])-[S;H0;+0:2]-[CH3;+0:11] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB. | Landgraf BJ, Arcinas AJ, Lee KH, Booker SJ | 2013 Oct 16 | 23991893 |
| MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. | Hernández HL, Pierrel F, Elleingand E, García-Serres R, Huynh BH, Johnson MK, Fontecave M, Atta M | 2007 May 1 | 17407324 |
| MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. | Pierrel F, Douki T, Fontecave M, Atta M | 2004 Nov 12 | 15339930 |