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EC Number Subunits Commentary Reference
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2? x * 28140, calculated from SDS-PAGE -, 726110
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2decamer - 675361, 676969
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2decamer 10 * 28112, calculation from nucleotide sequence, SDS-PAGE 392116
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2decamer 10*32000-35600, estimated by SDS-PAGE, confirmed by spectrometric analysis 676952
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2decamer five homodimer subunits 675382
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2dimer - 675361
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2dodecamer 12 * 28000, SDS-PAGE 741069
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2More enzyme forms a concentration-dependent decamer in solution, sedimentation velocity data 740763
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2More enzyme is a decamer of five dimers, crystallization data 740491
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2multimer x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes -, 701063
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