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EC Number Subunits Commentary Reference
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19? x * 53720, native enzyme, SDS-PAGE, x * 54790, sequence calculation 742430
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19? x * 54600, about, sequence calculation 742521
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19? x * 55000, about, sequence calculation 742521
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19? x * 64000 288079
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19dimer 2 * 51000, SDS-PAGE -, 288081
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19dimer 2 * 52000, SDS-PAGE -, 288082
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19dimer 2 * 95000, SDS-PAGE 288063
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19dimer plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site 742854
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19dimer x-ray crystallography 712753
Show all pathways known for 1.2.1.19Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.19monomer 1 * 55000, SDS-PAGE 656627
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