Literature summary for 5.3.99.2 extracted from

Kume, S.; Lee, Y.H.; Nakatsuji, M.; Teraoka, Y.; Yamaguchi, K.; Goto, Y.; Inui, T.
Fine-tuned broad binding capability of human lipocalin-type prostaglandin D synthase for various small lipophilic ligands (2014), FEBS Lett., 588, 962-969.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of GST-tagged enzyme mutant C65A/C167A, with truncated N-terminal 22-amino acid residues corresponding to the putative secretion signal peptide, in Escherichia coli strain BL21(DE3)	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C65A/C167A	site-directed mutagenesis, the mutation limits incorrect intra- and intermolecular disulfide bonds and protein aggregation during recombinant enzyme expression and purification	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P41222	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged truncated enzyme mutant C65A/C167A from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, and dialysis	Homo sapiens

Subunits

Subunits	Comment	Organism
More	three-dimensional structure of the enzyme and its hydrophobic cavaity, overview. The secondary structure elements of the enzyme comprise nine beta-strands and four alpha-helices	Homo sapiens

Synonyms

Synonyms	Comment	Organism
L-PGDS	-	Homo sapiens
lipocalin-type prostaglandin d synthase	-	Homo sapiens

General Information

General Information	Comment	Organism
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	Homo sapiens

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Release 2023.1 (January 2023)