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Results 1 - 10 of 11 > >>
EC Number Subunits Commentary Reference
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13? 39000, SDS-PAGE 650892
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13? x * 27945, calculation from nucleotide sequence 2081
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13? x * 27945, sequence calculation 748452
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13? x * 28000, SDS-PAGE 2081
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13? x * 45500 728034
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13dimer 2 * 28000, SDS-PAGE 2077, 2078
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13dimer crystallization studies 652886
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13homodimer 2 * 25000-30000, recombinant enzyme, SDS-PAGE -, 747721
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13homodimer comparisons of Picrophilus torridus enzyme structure with the Pyrococcus aspartate racemase structure. The dimerization interface is composed of three interaction surfaces, including an inter-subunit disulfide bond and contacts through the beta-sheets and alpha-helix. The interface between two molecules (Mol-A and Mol-B) of Picrophilus torridus PtoAspR looks similar to that of Pyrococcus aspartate racemase, except that there is no cysteine disulfide bond between two molecules of PtoAspR. Each subunit is composed of two homologous domains, the N-terminal domain with residues 1-101 and 207-232, and the C-terminal domain with residues 106-206. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains -, 747720
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13homodimer x-ray crystallography -, 716952
Results 1 - 10 of 11 > >>