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Literature summary for 2.1.1.297 extracted from

  • Wu, R.; Cao, Z.
    QM/MM study of catalytic methyl transfer by the N5-glutamine SAM-dependent methyltransferase and its inhibition by the nitrogen analogue of coenzyme (2008), J. Comput. Chem., 29, 350-357.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9WYV8
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Thermotoga maritima DSM 3109 Q9WYV8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 ?
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additional information 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 ?
-
?

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
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Thermotoga maritima