EC Number   |
Subunits |
Reference |
|---|
    3.5.1.18 | ? |
x * 43000, SDS-PAGE |
755172 |
| 3.5.1.18 | dimer |
2 * 41500, SDS-PAGE |
712756 |
| 3.5.1.18 | dimer |
the DapE enzyme exists in a dimeric form with each monomer consisting of a catalytic and dimerization domain |
734849 |
| 3.5.1.18 | dimer |
the enzyme is composed of catalytic and dimerization domains, the dimerization domain in DapE enzymes is required for catalysis |
735140 |
| 3.5.1.18 | homodimer |
2 * 41600, estimated from amino acid sequence |
719021 |
| 3.5.1.18 | homodimer |
2 * 42000, SD-PAGE |
719021 |
| 3.5.1.18 | monomer |
1 * 41350, electrospray mass spectroscopy |
-, 246565 |
| 3.5.1.18 | More |
the core of the catalytic domain consists of an eight-stranded twisted beta-sheet that is sandwiched between seven alpha-helices, active site structure and structure-activity relationship, overview |
712756 |
| 3.5.1.18 | More |
three-dimensional homology structure of the DapE, based on the crystal structure of the DapE from Neisseria meningitidis as template and and superimposed on the structure of the aminopeptidase from Aeromonas proteolytica, overview |
712506 |
