Literature summary extracted from

Shimamoto, S.; Yoshida, T.; Inui, T.; Gohda, K.; Kobayashi, Y.; Fujimori, K.; Tsurumura, T.; Aritake, K.; Urade, Y.; Ohkubo, T.
NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity (2007), J. Biol. Chem., 282, 31373-31379.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
5.3.99.2	-	Mus musculus

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
5.3.99.2	NMR solution structure, enzyme consists of an eight-stranded, antiparallel beta-barrel and a long alpha-helix associated with the outer surface of the barrel. The interior of the barrel forms a hydrophobic cavity containing two pockets. Prostaglandin H2 almost fully occupies hydrophilic pocket 1, in which C65 is located, and all-trans retinoic acid occupies hydrophilic pocket 2	Mus musculus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
5.3.99.2	retinoic acid	non-competitive	Mus musculus

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.3.99.2	Mus musculus	O09114	recombinant protein	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)