LTD4 is converted to LTE4 by DPEP1/2

Stable Identifier
R-HSA-266012
Type
Reaction
Species
Homo sapiens
Compartment
Synonyms
Further cleavage of LTD4 forms LTE4
Locations in the PathwayBrowser
Summation

Another outer surface membrane-bound, homodimeric enzyme, dipeptidase, existing in two forms DPEP1 (Adachi et al. 1989) and DPEP2 (Lee et al. 1983, Raulf et al. 1987), further hydrolyses leukotriene D4 (LTD4) to leukotriene E4 (LTE4), cleaving a glycine residue in the process.

Literature References
PubMed ID Title Journal Year
3563417 Release and functional characterization of the leukotriene D4-metabolizing enzyme (dipeptidase) from human polymorphonuclear leucocytes

Raulf, M, König, W, Köller, M, Stüning, M

Scand J Immunol 1987
6293969 Conversion of leukotriene D4 to leukotriene E4 by a dipeptidase released from the specific granule of human polymorphonuclear leucocytes

Lee, CW, Lewis, RA, Corey, EJ, Austen, KF

Immunology 1983
2768222 Purification and characterization of human microsomal dipeptidase

Adachi, H, Kubota, I, Okamura, N, Iwata, H, Tsujimoto, M, Nakazato, H, Nishihara, T, Noguchi, T

J Biochem 1989
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
dipeptidase activity of DPEP1,2,3 dimers [plasma membrane]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed