EC Number   |
Subunits  |
Reference |
|---|
    1.14.17.1 | ? |
x * 68480, predicted |
715066 |
| 1.14.17.1 | ? |
x * 70000-75000, Western blot analysis, recombinant enzyme |
438627 |
| 1.14.17.1 | ? |
x * 72000, secreted and modified (N-glycosylation) form, Western blot analysis |
715661 |
| 1.14.17.1 | ? |
x * 75000, SDS-PAGE of reduced and carboxymethylated MDBH |
438597 |
| 1.14.17.1 | dimer or tetramer |
the enzyme occurs borh as dimer and tetramer, which can be separated by size exclusion chromatography. The dimer and tetramer do not interconvert in the pH interval pH 4-9. Under denaturing conditions, the tetramer converts to a dimer, and upon addition of a reducing agent, the dimer converts to a monomer. The dimeric structure is asymmetric. In the A chain, the two catalytic CuH and CuM domains are in a closed conformation, and in the B chain, they adopt the same open conformation as seen in peptidylglycine alpha-hydroxylating (and alpha-amidating) monooxygenase (PHM), the catalytic CuH domain in chain A is moved away from the DOMON domain and closer to the catalytic CuM domain. The DOMON domain has an immunoglobulin (Ig)Βlike beta-sandwich structure, the catalytic core (the CuH and CuM domains) has the same topology as the structure of PHM, and the dimerization domains consisting of two antiparallel alpha helices form a four-helix bundle. Following the dimerization domain, there is a beta-strand (residues 561 to 566) taking part in the catalytic CuM domain and a beta-strand (residues 608 to 614) that is part of the DOMON domain, creating a very integrated structure, coordinating residues are Asp99, Leu100, Ala115, and Asp130. The DOMON domain and the dimerization domain are linked via C154-C596. Chain A is linked via two intermolecular disulfide bonds with chain B in the dimerization domain. Enzyme structure analysis, detailed overview |
746431 |
| 1.14.17.1 | More |
the enzyme contains a DOMON domain, a Cu2_monooxygen domain, and three glycosylation sites |
744949 |
| 1.14.17.1 | tetramer |
4 * 65000, deduced from cDNA |
438634 |
| 1.14.17.1 | tetramer |
4 * 66000-74000, SDS-PAGE after cleavage of intersubunit disulfide bonds with dithiothreitol, tetramer consists of two disulfid-linked dimers |
438629 |
| 1.14.17.1 | tetramer |
4 * 72000 SDS-PAGE |
438602 |
| 1.14.17.1 | tetramer |
4 * 80000, SDS-PAGE after treatment with 2-mercaptoethanol, subunits joined in pairs by disulfide bonds |
438603 |
