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EC Number Subunits Commentary Reference
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23trimer - 643073, 643075, 643076
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23monomer 1 * 50000, SDS-PAGE, 1 * 49624, calculated from the deduced amino acid sequence, native mass by gel filtration 662429
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23monomer 1 * 58300, SDS-PAGE 721526
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23dimer 1 * 64000 + 1 * 57000 643069
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23dimer 2 * 33000, SDS-PAGE, gel filtration 643067
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23dimer 2 * 64000, SDS-PAGE, gel filtration 643065
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23trimer 3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer) -, 288688
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23More C324 does not form a disulphide bond with any other cysteine. This is consistent with the replacement of C307 by a serine in Y. pestis and the great distance between the three other cysteines (C296, C301 and C385) and C324 -, 735569
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23trimer crystal structure analysis 643073
Show all pathways known for 2.7.7.23Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.23trimer GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein 740866
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