Literature summary for 2.1.1.28 extracted from

Hou, Q.Q.; Wang, J.H.; Gao, J.; Liu, Y.J.; Liu, C.B.
QM/MM studies on the catalytic mechanism of phenylethanolamine N-methyltransferase (2012), Biochim. Biophys. Acta, 1824, 533-541.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants

Protein Variants	Comment	Organism
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
E219Q	mutation has little effect on the kcat value. The bridge water still forms two hydrogen bonds between Gln219 and Glu185	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
SK&F 29661	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + noradrenaline	-	Homo sapiens	S-adenosyl-L-homocysteine + epinephrine	-	?

Synonyms

Synonyms	Comment	Organism
PNMT	-	Homo sapiens

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Release 2023.1 (January 2023)