Enzymes
| UniProtKB help_outline | 2,834 proteins |
Reaction participants Show >> << Hide
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 868 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
uridine54 in tRNA
Identifier
RHEA-COMP:10193
Reactive part
help_outline
- Name help_outline UMP residue Identifier CHEBI:65315 Charge -1 Formula C9H10N2O8P Positionhelp_outline 54 SMILEShelp_outline C1=CC(NC(N1[C@@H]2O[C@H](COP(*)(=O)[O-])[C@H]([C@H]2O)O*)=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 73 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
5-methyluridine54 in tRNA
Identifier
RHEA-COMP:10167
Reactive part
help_outline
- Name help_outline 5-methyluridine 5'-phosphate residue Identifier CHEBI:74447 Charge -1 Formula C10H12N2O8P Positionhelp_outline 54 SMILEShelp_outline [C@@H]1(N2C(NC(=O)C(=C2)C)=O)O[C@H](COP(*)(=O)[O-])[C@H]([C@H]1O)O* 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 792 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:42712 | RHEA:42713 | RHEA:42714 | RHEA:42715 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Enzymatic mechanism of tRNA (m5U54)methyltransferase.
Kealey J.T., Gu X., Santi D.V.
tRNA (m5U54)methyltransferase (RUMT) catalyzes the methylation of uridine 54 of transfer RNA by S-adenosyl-L-methionine. In this report, we present the enzymatic mechanism of RUMT, including the stereochemical course of the methylation reaction, and discuss RUMT-tRNA recognition. As part of its en ... >> More
tRNA (m5U54)methyltransferase (RUMT) catalyzes the methylation of uridine 54 of transfer RNA by S-adenosyl-L-methionine. In this report, we present the enzymatic mechanism of RUMT, including the stereochemical course of the methylation reaction, and discuss RUMT-tRNA recognition. As part of its enzymatic mechanism, we postulate that RUMT catalyzes the disruption of RNA-RNA contacts. We also show that many nucleotide substitutions can be made in the T-loop of tRNA without affecting RUMT binding, indicating that the recognition of the T-loop by RUMT is not stringent. << Less
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Isolation and chracterization of m5U-methyltransferase from Escherichia coli.
Greenberg R., Dudock B.
The tRNA-modifying enzyme, S-adenosylmethionine: tRNA (uridine-5)-methyltransferase, has been purified essentially to homogeneity from an Escherichia coli strain containing an elevated level of this enzyme. A rapid, efficient method has been developed for the purification, consisting of polyethyle ... >> More
The tRNA-modifying enzyme, S-adenosylmethionine: tRNA (uridine-5)-methyltransferase, has been purified essentially to homogeneity from an Escherichia coli strain containing an elevated level of this enzyme. A rapid, efficient method has been developed for the purification, consisting of polyethyleneimine precipitation to remove nucleic acids, followed by phosphocellulose and Blue Sepharose affinity chromatography. The enzyme is a single polypeptide chain of molecular weight 42,000. It has a pH optimum of 8.4, a Km of 12.5 microM for S-adenyosyl-L-methionine, and a Km of 1.1 microM for wheat germ tRNAGly1. The ability of the enzyme to methylate a variety of tRNA substrates including prokaryotic, eukaryotic, mitochondrial, and chloroplastic tRNAs has been characterized. << Less