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 16 > >>
EC Number
crystallographic data. Tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine
x * 14100, pi-protein, calculated from the amino acid sequence
active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein
4 * 14000
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE
x * 58000, SDS-PAGE
x * 13800, SDS-PAGE
two tetramers forming a pseudo fourfold rotational symmetry, the enzyme protein shows a double-psi beta-barrel structure
Results 1 - 10 of 16 > >>