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Results 1 - 3 of 3
EC Number Reaction Commentary Reference
Show all pathways known for 2.1.1.28Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.28S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine ordered sequential reaction 639436
Show all pathways known for 2.1.1.28Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.28S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine random binding mechanism with a kinetically preferred order of binding where S-adenosyl-L-methionine is the preferred first substrate 639431
Show all pathways known for 2.1.1.28Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.28S-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 718999
Results 1 - 3 of 3