EC Number   |
Reference |
|---|
    2.1.1.5 | - |
673003 |
| 2.1.1.5 | by multiple anomalous diffraction |
673003 |
| 2.1.1.5 | crystals with P2(1) symmetry, assymetric unit contains the whole functional tetramer showing point symmetry 222 |
659712 |
| 2.1.1.5 | dominant structural feature of wild type BHMT is an (betaalpha)8 barrel. A modeled structure of truncated BHMT suggests that this protein would assume a horseshoe fold and lack methyltransferase activity |
733936 |
| 2.1.1.5 | molecular dynamics simulations predict that K+ ions interact with residues Asp26 and/or Glu159. Crystal structure of BHMT bound to homocysteine confirms these sites of interaction and reveals further contacts between K+ ions and BHMT residues Gly27, Gln72, Gln247, and Gly298 |
735230 |
| 2.1.1.5 | recombinant enzyme |
441239, 441240 |
