Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | isoform HemK methylates peptide release factors RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and hemK is required for the methylation within the same fragment of, at least, RF1 in vivo | ? | - |
? | |
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine | Escherichia coli | - |
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine | - |
? | |
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine | Escherichia coli | - |
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0ACC1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | isoform HemK methylates peptide release factors RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and hemK is required for the methylation within the same fragment of, at least, RF1 in vivo | Escherichia coli | ? | - |
? | |
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine | - |
Escherichia coli | S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine | - |
? | |
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine | - |
Escherichia coli | S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | a hemK knockout suffers severe growth defects and shows a global shift in gene expression to anaerobic respiration. This shift may lead to the abrogation of photosensitivity by reducing the oxidative stress. Suppressor mutations that abrogate the growth defects of the hemK knockout strain are caused by a threonine to alanine change at codon 246 of polypeptide chain release factor RF2, indicating that hemK plays a role in translational termination. The hemK knockout strain shows an enhanced rate of read-through of nonsense codons and induction of transfer-mRNA-mediated tagging of proteins within the cell. HemK methylates RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and hemK is required for the methylation within the same fragment of, at least, RF1 in vivo | Escherichia coli |