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EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.12? x * 46000, SDS-PAGE 648805
Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.12? x * 85000, SDS-PAGE 648808
Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.12More structure-function relationship, overview 706613
Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.12trimer the tertiary structure is stabilized by hydrogen bonds and a hydrophobic core, three beta-sheets and six alpha-helices surround a traversing channel with dominant positive charge in the middle of the trimer, structure, overview. The enzyme contains a Cys-Xaa-Xaa-Cys motif required for oxido-reductase activity and MIF-like activities like glucorticoid overriding and cell proliferation 703331
Display the word mapDisplay the reaction diagram Show all sequences 5.3.3.12trimer trimer formation is required for MIF tautomerase activity, trimer three-dimensional structure and tautomerase active site structure. The subunit interface is not as hydrophobic as the interior of the monomer, however, there is a hydrophobic patch on the surface involving residues Y36, Y95, W108, and F113, MALDI-TOF and analytical gel filtration analysis, overview 702357
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