EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.1.28 | model is prepared on the basis of X-ray crystal structure of hPNMT in complex with S-adenosyl-L-homocysteine (AdoHcy) and the inhibitor SK&F 29661 | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.1.1.28 | E185Q | mutant has the same Km value as the wild-type hPNMT but extremely lower kcat value. E185Q mutation presents obvious structural changes in the active site | Homo sapiens |
2.1.1.28 | E219Q | mutation has little effect on the kcat value. The bridge water still forms two hydrogen bonds between Gln219 and Glu185 | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.28 | SK&F 29661 | - |
Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.28 | Homo sapiens | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.1.1.28 | S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine | to elucidate the detailed mechanism of enzymatic catalysis of PNMT, combined quantum-mechanical/molecular-mechanical (QM/MM) calculations are performed. The calculation results reveal that this catalysis contains three elementary steps: the deprotonation of protonated norepinphrine, the methyl transferring step and deprotonation of the methylated norepinphrine. The methyl transferring step is proved to be the rate-determining step undergoing a SN2 mechanism with an energy barrier of 16.4 kcal/mol | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.28 | S-adenosyl-L-methionine + noradrenaline | - |
Homo sapiens | S-adenosyl-L-homocysteine + epinephrine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.28 | PNMT | - |
Homo sapiens |