EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.1.1.297 | more |
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 |
? |
- |
? |
2.1.1.297 | more |
PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln |
Chlamydia trachomatis |
? |
- |
? |
2.1.1.297 | more |
no evidence for a DNA adenine-methyltransferase activity |
Mus musculus |
? |
- |
? |
2.1.1.297 | more |
PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln |
Chlamydia trachomatis |
? |
- |
? |
2.1.1.297 | more |
the catalytic methyl transfer by methyltransferase HemK is an energy-favored process with an activation barrier of 15.7 kcal/mol and an exothermicity of 12.0 kcal/mol, while the coenzyme-modified HemK is unable to catalyze the methyl transfer because of a substantial barrier of 20.6 kcal/mol and instability of the product intermediate. Therefore the nitrogen analogue of the SAM coenzyme should be a practicable inhibitor for the catalytic methyl transfer by HemK. The protein environment, especially the residues Asn197 and Pro198 in the active site, plays a pivotal role in stabilizing the transition state and regulating the positioning of reactive groups |
Thermotoga maritima |
? |
- |
? |
2.1.1.297 | more |
the catalytic methyl transfer by methyltransferase HemK is an energy-favored process with an activation barrier of 15.7 kcal/mol and an exothermicity of 12.0 kcal/mol, while the coenzyme-modified HemK is unable to catalyze the methyl transfer because of a substantial barrier of 20.6 kcal/mol and instability of the product intermediate. Therefore the nitrogen analogue of the SAM coenzyme should be a practicable inhibitor for the catalytic methyl transfer by HemK. The protein environment, especially the residues Asn197 and Pro198 in the active site, plays a pivotal role in stabilizing the transition state and regulating the positioning of reactive groups |
Thermotoga maritima DSM 3109 |
? |
- |
? |
2.1.1.297 | more |
PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln |
Chlamydia trachomatis ATCC VR-902B |
? |
- |
? |
2.1.1.297 | more |
PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln |
Chlamydia trachomatis ATCC VR-902B |
? |
- |
? |
2.1.1.297 | S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine |
- |
Thermotoga maritima |
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine |
- |
? |
2.1.1.297 | S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine |
- |
Thermotoga maritima DSM 3109 |
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine |
- |
? |