Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Subunits

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 17 > >>
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12? x * 100000, SDS-PAGE 758221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12? x * 110500, calculated from amino acid sequence 758221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12? x * 130000, His6-tagged enzyme, SDS-PAGE 757973
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12? x * 164000, SDS-PAGE 755703
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12? x * 93000 + x * 83000, subunits AcsB and AcsA, SDS-PAGE -, 758133
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12dimer alphabeta, 1 * 83000 + 1 * 93000, SDS-PAGE 637175
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12dimer BcsA and BcsB form a 1:1 stoichiometric complex spanning approximately 150 A perpendicular and 55 A parallel to the membrane. The complex is divided into a cuboid-shaped membrane-spanning region sandwiched between large cytoplasmic and periplasmic domains. BcsA contains four N-terminal and four C-terminal transmembrane-helices separated by a large intracellular loop (4/5-loop) that forms a GT-domain (aa 128 to 368). transmembrane domains 3-8 form a narrow channel for the translocating polysaccharide and BcsA's intracellular C-terminus (aa 575 to 759) contains a 6-stranded beta-barrel and a highly curved alpha-helical region that attaches the beta-barrel to the GT-domain. BcsB is a dome-shaped, beta-strand rich, periplasmic protein. Its N-terminal region forms the tip of the dome, whereas the C-terminal transmembrane-anchor interacts with BcsA. Two amphipathic helices further stabilize its interaction with BcsA and the periplasmic water-membrane interface. Domain structures. Modeling, overview 736877
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12dimer recombinant catalytic domains of rice CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. The monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain, structure comparison and modeling, overview. Proposed role for dimers in particle rosette assembly 736991
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12homodimer isozyme CESA4 703730
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12monomer isozyme CESA7 703730
Results 1 - 10 of 17 > >>