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EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.135monomer 1 × 25000, fully active catalytically 638617
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.135monomer 1 × 25300, SDS-PAGE in presence of 2-mercaptoethanol, fully active catalytically 638617
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.135monomer 1 × 25800, fully active catalytically 638619
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.135More epitope mapping, the enzyme contains a C-terminal transmembrane domain 674832
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.135More LRAT monomer interact in membranes and form functional homodimers, the dimer formation is mediated by disulfide bond formation and protein-protein interactions 638623
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.135More the enzyme exists as a mixture of monomer and dimer, determined by sedimentation equilibrium analysis and mass spectrometry, higher aggregation, up to pentamers, occurs in absence of denaturing agents 658001
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