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EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Commentary Reference
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.2-999 - up to 480000 kDa, quarternary structure changes drastically with buffer environment 392113
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.225000 - 8 * 25000 SDS-PAGE 392146
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.228000 - - 741069
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.228000 - monomer, SDS-PAGE 392116
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.228112 - 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 1.5.1.228140 - 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 1.5.1.228500 - 10-12 * 28500 392148
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.230000 - - 392113
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.230000 - SDS-PAGE 392112, 392139
Show all pathways known for 1.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.230000 - 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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