5.3.99.2	evolution	the enzyme belongs to the lipocalin superfamily	726907	
5.3.99.2	evolution	the enzyme is a member of the lipocalin superfamily	726906	
5.3.99.2	malfunction	co-localization of arrestin-3 with L-PGDS is drastically reduced in MG-63 cells when L-PGDS activity is inhibited	715626	
5.3.99.2	malfunction	dextran sodium sulfate treatment to L-PGDS-deficient
mice shows lower ulcerative colitis disease activity than control mice	713720	
5.3.99.2	malfunction	double knockout mice, lacking lipocalin prostaglandin D synthase as well as PPARgamma2, have impaired carbohydrate and lipid metabolism with glucose tolerance compared to any other genotypes, their interscapular brown adipose tissue exhibits greater lipid content than that of wild-type mice, which is independent of PPARgamma2 dysfunction. In subcutaneous white adipose tissue, L-PGDS KO mice exhibit a 4fold increase in UCP1 expression and a reduction in adipogenic marker aP2 expression. Phenotypes, overview	-, 728575	
5.3.99.2	malfunction	enzyme deficiency accelerates the growth of melanoma in mice. Enzyme deficiency results in functional changes of tumor endothelial cells such as accelerated vascular hyperpermeability, angiogenesis, and endothelial-to-mesenchymal transition in tumors, which in turn reduce tumor cell apoptosis	748450	
5.3.99.2	malfunction	the incidence of preterm birth is significantly reduced to 40% in enzyme-deficient knockout mice	749210	
5.3.99.2	malfunction	the stable transfection with antisense L-PGDS induces markedly the stimulation of fat storage in cultured adipocytes during the maturation phase	714066	
5.3.99.2	additional information	analysis of enzyme structure in complex with substrate analogue U44069, 9,11-epoxymethano-PGH2, and in ligand-free form. The catalytic Cys 65 thiol group occurs in two different conformations, each making a distinct hydrogen bond network to neighboring residues, mechanism of the cysteine nucleophile activation, and modelling of dynamics of protein-substrate and protein-product interactions, overview	728090	
5.3.99.2	additional information	binding of various lipophilic ligands in the hydrophobic cavity of lipocalin-type prostaglandin D synthase, i.e. hemin, biliverdin, and bilirubin, retinoids (all-trans and 9-cis retinoic acids), thyroids, steroids (progesterone, testosterone, and corticosterone), flavonoids (genistein, naringenin, and daidzein), the substrate PGH2 analogue U46619, and the fluorescence probe TNS, buffer-independent thermodynamic parameters, overview. The broad binding capability of the enzyme for ligands is realized by hydrophilic interactions delicately tuned by enthalpy-entropy compensation using combined effects of hydrophilic and hydrophobic interactions	727534