2.1.1.297: peptide chain release factor N5-glutamine methyltransferase
This is an abbreviated version!
For detailed information about peptide chain release factor N5-glutamine methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.297
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2.1.1.297
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histone
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coactivator
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coactivator-associated
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methyltransferases
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prmts
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dimethylarginine
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h3r2me2a
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sdmas
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picln
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di-methylation
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h4r3me2s
- 2.1.1.297
- histone
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coactivator
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coactivator-associated
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methyltransferases
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prmts
- dimethylarginine
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h3r2me2a
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sdmas
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picln
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di-methylation
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h4r3me2s
Reaction
Synonyms
HemK, HemK methyltransferase family member 2, isoform CRA_c, Hemk1, Hemk2, N5-glutamine methyltransferase, N5-glutamine MTase, N5-glutamine S-adenosyl-L-methionine dependent methyltransferase, N6AMT1, PrmC, PrmC/HemK, release factor glutamine methyltransferase, TM0488
ECTree
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Substrates Products
Substrates Products on EC 2.1.1.297 - peptide chain release factor N5-glutamine methyltransferase
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REACTION DIAGRAM
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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?
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
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?
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
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?
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
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?
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
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?
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
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-
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?
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
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?
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PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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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
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additional information
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Q6PRU9
no evidence for a DNA adenine-methyltransferase activity
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additional information
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no evidence for a DNA adenine-methyltransferase activity
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additional information
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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
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additional information
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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
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