EC Number   |
|---|
    2.1.1.28 | - |
| 2.1.1.28 | 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 |
| 2.1.1.28 | 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)] |
| 2.1.1.28 | 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. |
| 2.1.1.28 | 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. |
| 2.1.1.28 | 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 |
| 2.1.1.28 | 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 |
| 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 |
| 2.1.1.28 | 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 |
