EC Number   |
Title |
Organism |
|---|
   2.8.4.4 | A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein |
Escherichia coli |
| 2.8.4.4 | A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein |
Escherichia coli W3110 / ATCC 27325 |
| 2.8.4.4 | Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily |
Escherichia coli |
| 2.8.4.4 | Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB |
Thermotoga maritima |
| 2.8.4.4 | Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB |
Thermotoga maritima DSM 3109 |
| 2.8.4.4 | Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase |
Thermotoga maritima |
| 2.8.4.4 | Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase |
Thermotoga maritima DSM 3109 |
| 2.8.4.4 | Redox behavior of the S-adenosylmethionine (SAM)-binding Fe-S cluster in methylthiotransferase RimO, toward understanding dual SAM activity |
Thermotoga maritima |
| 2.8.4.4 | RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli |
Escherichia coli |
| 2.8.4.4 | Stereochemical course of the reaction catalyzed by RimO, a radical SAM methylthiotransferase |
Bacteroides thetaiotaomicron |
