CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Prostaglandin reductase 2

Enzyme Information

1.3.1.-
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt Q9EQZ5
1.3.1.74
2-alkenal reductase (NAD(P)(+)).
based on mapping to UniProt Q9EQZ5
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
-!- Highly specific for 4-hydroxynon-2-enal and non-2-enal. -!- Alk-2-enals of shorter chain have lower affinities. -!- Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one. -!- Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid. -!- Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
1.3.1.48
15-oxoprostaglandin 13-reductase.
based on mapping to UniProt Q9EQZ5
11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)(+) = (5Z)-(13E)-11- alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.
-!- Reduces 15-oxoprostaglandins to 13,14-dihydro derivatives. -!- The enzyme from placenta is specific for NAD(+).

UniProtKB Entries (1)

Q9EQZ5
PTGR1_CAVPO
Cavia porcellus
Prostaglandin reductase 1

PDB Structure

PDB 1V3V
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-Oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop
Hori, T., Yokomizo, T., Ago, H., Sugahara, M., Ueno, G., Yamamoto, M., Kumasaka, T., Shimizu, T., Miyano, M.
J.Biol.Chem.