Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.1.1.28: phenylethanolamine N-methyltransferase

This is an abbreviated version!
For detailed information about phenylethanolamine N-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.28

Reaction

S-adenosyl-L-methionine
+
phenylethanolamine
=
S-adenosyl-L-homocysteine
 +
N-Methylphenylethanolamine

Synonyms

hPNMT, methyltransferase, noradrenaline N-, NMT, noradrenalin methyltransferase, noradrenalin N-methyltransferase, noradrenaline N-methyltransferase, norepinephrin N-methyltransferase, norepinephrine methyltransferase, norepinephrine N-methyltransferase, phenethanolamine methyltransferase, phenethanolamine N-methyltransferase, PNMT

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.28 phenylethanolamine N-methyltransferase

Crystallization

Crystallization on EC 2.1.1.28 - phenylethanolamine N-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in complex with an inhibitor and the cofactor product S-adenosyl-L-homocysteine using hanging-drop technique with PEG 6000 and lithium chloride as precipitant
-
hanging drop vapor diffusion using drops of 1 microl of protein and 1 microl of precipitant over 100 microl of precipitant [ 5-8% PEG 6K, 0.25 M LiCl, and 0.1 M sodium cacodylate (pH 5.5-6.0)]
hanging drop vapour diffusion method is used with 2 mircol drops on 3 M sealed over 500 mircol or 100 microl precipitant in 24-well or 96-well trays. In the absence of reducing agents crystals grow on protein concentrations of 30 to 40 mg/ml and appear in two or three days. The addition of DTT inhibits formation of crystals under the same condition. Reduced and oxidized glutathione are added to PEG/LiCl crystallisation conditions, crystals only grow in drops where the amount of oxidized glutathione is higher than reduced, the ratio of 1:20 (reduced glutathione/oxidized glutathione) gives the largest crystals.
-
hanging drop vapour diffusion on 3 M tape with 1 microl protein/ligand mixture plus 1 microl precipitant over 100 microl precipitant (0.6-0.8 M NH4H2PO4, 0.1 M citrate pH 5.3-5.8). The human phenylethanolamine N-methyltransferase S-adenosyl-L-homocysteine SKF 64139 structure is solved by difference Fourier methods and refines at 2.4 A resolution. A hydrophilic inhibitor does not bind in a distinclty differnt orientation than a hydrophobic inhibitor.
in complex with inhibitors 3-hydroxymethyl-7-nitro-1,2,3,4-tetrahydroisoquinoline, 7-bromo-3-hydroxymethyl-1,2,3,4-tetrahydroisoquinoline, 3-hydroxyethyl-7-nitro-1,2,3,4-tetrahydroisoquinoline, 3-hydroxypropyl-7-nitro-1,2,3,4-tetrahydroisoquinoline
-
in complex with S-adenosyl-L-homocysteien and either 7-iodo-1,2,3,4-tetrahydroisoquinoline or 8,9-dichloro-2,3,4,5-tetrahydro-1H-2-benzazepine or 7-sulfonamido-1,2,3,4-tetrahydroisoquinoline
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
-
purified recombinant His6-tagged wild-type and mutant K75A enzymes in complex with S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, and with inhibitors (R)-4, (R)-5, (R)-6, and (R)-7, X-ray diffraction structure determination and analysis at 2.0-2.8 A resolution
-