EC Number |
Protein Variants |
Reference |
---|
5.3.3.12 | G486R |
slaty light mutation, 28fold reduction in enzyme activity, sliding of transmembrane domain towards N-terminus of protein thus interfering with the active site. Increase in pheomelanin and reduction in eumelanin produced by melanocytes in culture |
661009 |
5.3.3.12 | more |
enzyme knockout mutant, animals are viable and do not show any abnormalities in skin, retinal pigment epithelium, or brain. Animals show a diluted coat colour phenotype due to reduced melanin content in hair. Primary melanocytes from knockout animals are viable in culture and show a normal distribution of tyrosinase and tyrosinase-related protein 1 |
662850 |
5.3.3.12 | more |
modification of Pro1, e.g. via isothiocyanate inhibitors, alters the tertiary, but not the secondary or quaternary, structure of the trimer without affecting its thermodynamic stability, overview |
702357 |
5.3.3.12 | more |
preparation of biotin-isothiocyanate-labeled enzyme, proteomic screening in recombinant HeLa cells and identification of the modification site by mass spectrometry |
702139 |
5.3.3.12 | P1G |
generation of knockout mice in which the endogenous mif gene is replaced by one encoding a tautomerase-null, Pro1-Gly1 MIF protein, i.e. P1G-MIF, which is P1G-MIF is catalytically completely inactive, but maintains significant, albeit reduced, binding to its cell surface receptor CD74 and to the intracellular binding protein JAB1/CSN5. Mutant mice show a phenotype in assays of growth control and tumor induction that is intermediate between those of the wild type mif+/+ and complete MIF deficiency mif-/-, overview. Reduced development of benzo[alpha]pyrene-induced skin tumors in mif-deficient mice |
705691 |
5.3.3.12 | P1G |
inactive |
727347 |
5.3.3.12 | R194Q |
slaty mutation, 3fold reduction in enzyme activity compared to wild-type. Increase in pheomelanin and reduction in eumelanin produced by melanocytes in culture |
661009 |