Inhibitors | Comment | Organism | Structure |
---|---|---|---|
hemin | Fe3+-heme, inhibits arginyl-transferase through a redox mechanism that involves the formation of disulfide between the enzymes Cys-71 and Cys-72 residues | Mus musculus | |
hemin | Fe3+-heme, inhibits arginyl-transferase through a redox mechanism that involves the formation of disulfide between the enzymes Cys-71 and Cys-72 residues | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginyl-tRNAArg + protein | Mus musculus | - |
tRNAArg + L-arginyl-[protein] | - |
? | |
L-arginyl-tRNAArg + protein | Saccharomyces cerevisiae | - |
tRNAArg + L-arginyl-[protein] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginyl-tRNAArg + protein | - |
Mus musculus | tRNAArg + L-arginyl-[protein] | - |
? | |
L-arginyl-tRNAArg + protein | - |
Saccharomyces cerevisiae | tRNAArg + L-arginyl-[protein] | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Arg-tRNA-protein transferase | - |
Mus musculus |
Arg-tRNA-protein transferase | - |
Saccharomyces cerevisiae |
arginyl-transferase | - |
Mus musculus |
arginyl-transferase | - |
Saccharomyces cerevisiae |
Ate1 | - |
Mus musculus |
Ate1 | - |
Saccharomyces cerevisiae |
R-transferase | - |
Mus musculus |
R-transferase | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | N-terminal arginylation of intracellular proteins by Arg-tRNA-protein transferase is a part of the N-end rule pathway of protein degradation | Mus musculus |
physiological function | N-terminal arginylation of intracellular proteins by Arg-tRNA-protein transferase is a part of the N-end rule pathway of protein degradation | Saccharomyces cerevisiae |