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 - 8 of 8
EC Number Subunits Commentary Reference
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282dimer - -, 644536, 739956
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282dimer 2 * 31350, wild type enzyme, gel filtration 656292
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282dimer distinct mode of dimerization in which the individual molecules interact in a back-to-front manner, overview. The molecules of the RifI2 dimer associate via hydrophobic interactions between residues on alpha-helix alpha8 of the first molecule and alpha10' of the second molecule. In addition, the side chain of Gln167 on apha-helix alpha8 forms a hydrogen bond with the guanidinium group of Arg243' on beta-strand beta10'. A second hydrogen bond to Arg243' may be made by Asn171. Asp53 and Arg56 on alpha-helix alpha2 bind the imidazole ring of His31' on alpha-helix alpha1' -, 740100
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282homodimer - 644537
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282homodimer 2 * 30000, about, recombinant enzyme, SDS-PAGE -, 724089
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282monomer 1 * 31500, SDS-PAGE -, 654384
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282monomer 1 * 41000 286356
Show all pathways known for 1.1.1.282Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.282More enzyme three-dimensional structure determination, analysis, and comparisons, overview. The N-terminal or catalytic domain comprises residues 1 to 113 and 256 to 283, whereas the C-terminal or nucleotide-binding domain is build up of residues 114 to 255. The catalytic domain forms an open alpha/beta sandwich, which is characteristic for enzymes of the SDH/QDH family. The substrate-binding site is located in the N-terminal domain, close to the nicotinamide ring of the cofactor -, 727115
Results 1 - 8 of 8