EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.297 | Thermotoga maritima | Q9WYV8 | - |
- |
2.1.1.297 | Thermotoga maritima DSM 3109 | Q9WYV8 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.297 | 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 | ? | - |
? | |
2.1.1.297 | 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 | ? | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.297 | S-adenosyl-L-methionine | - |
Thermotoga maritima |