Dipeptidase 2

DPEP2
Identifiers
Aliases	DPEP2, MBD2, dipeptidase 2
External IDs	OMIM: 609925; MGI: 2442042; HomoloGene: 49703; GeneCards: DPEP2; OMA:DPEP2 - orthologs
Gene location (Human)
Chr.	Chromosome 16 (human)
End	68,000,586 bp
RNA expression pattern
	Top expressed in
	granulocyte; ; monocyte; ; blood; ; spleen; ; right lung; ; lymph node; ; bone marrow; ; upper lobe of left lung; ; testicle; ; appendix;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	peptidase activity; metalloexopeptidase activity; dipeptidyl-peptidase activity; metallopeptidase activity; hydrolase activity; metal ion binding; dipeptidase activity;
Cellular component	anchored component of membrane; membrane;
Biological process	proteolysis;
	Sources:Amigo / QuickGO
Orthologs
	64174
	319446
	ENSG00000167261
	ENSMUSG00000053687
	Q9H4A9
	Q8C255
	NM_022355; NM_001324159; NM_001369657
	NM_001301204; NM_001301205; NM_176913
	NP_001311088; NP_071750; NP_001356586
	NP_001288133; NP_001288134; NP_795887
	Wikidata
View/Edit Human	View/Edit Mouse

Dipeptidase 2 (DPEP2) is a protein which in humans is encoded by the DPEP2 gene.^[4]

DPEP2 belongs to the membrane-bound dipeptidase (EC 3.4.13.19) family. These enzymes hydrolyze a variety of dipeptides, including leukotriene D₄, the beta-lactam ring of some antibiotics, and cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000167261 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Habib GM, Shi ZZ, Cuevas AA, Lieberman MW (July 2003). "Identification of two additional members of the membrane-bound dipeptidase family". The FASEB Journal. 17 (10): 1313–5. doi:10.1096/fj.02-0899fje. PMID 12738806. S2CID 15252871.
^ "Entrez Gene: Dipeptidase 2".

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Metabolism: lipid metabolism – eicosanoid metabolism enzymes
Precursor	Phospholipase A2 Phospholipase C Diacylglycerol lipase
Prostanoids	Cyclooxygenase PTGS1 PTGS2 PGD2 synthase PGE synthase Prostaglandin-E2 9-reductase PGI2 synthase TXA synthase
Leukotrienes	5-Lipoxygenase activating protein/Arachidonate 5-lipoxygenase LTA4 hydrolase (B4 synthesis) LTC4 synthase Gamma-glutamyl transpeptidase LTD4 hydrolase
Ungrouped	HPGD