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EC Number
Subunits
Commentary
Reference
?
x * 68480, predicted
?
x * 70000-75000, Western blot analysis, recombinant enzyme
?
x * 72000, secreted and modified (N-glycosylation) form, Western blot analysis
?
x * 75000, SDS-PAGE of reduced and carboxymethylated MDBH
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)–like 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
More
the enzyme contains a DOMON domain, a Cu2_monooxygen domain, and three glycosylation sites
tetramer
4 * 65000, deduced from cDNA
tetramer
4 * 66000-74000, SDS-PAGE after cleavage of intersubunit disulfide bonds with dithiothreitol, tetramer consists of two disulfid-linked dimers
tetramer
4 * 72000 SDS-PAGE
tetramer
4 * 80000, SDS-PAGE after treatment with 2-mercaptoethanol, subunits joined in pairs by disulfide bonds
Results 1 - 10 of 11 > >>