Structural highlights
Function
DPEP1_PIG Hydrolyzes a wide range of dipeptides (PubMed:8045301, PubMed:8823187). Hydrolyzes the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Also possesses beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics (By similarity).[UniProtKB:P31428][1] [2] Independently of its dipeptidase activity, acts as an adhesion receptor for neutrophil recruitment from bloodstream into inflamed lungs and liver.[UniProtKB:P31428]
References
- ↑ Keynan S, Hooper NM, Turner AJ. Directed mutagenesis of pig renal membrane dipeptidase. His219 is critical but the DHXXH motif is not essential for zinc binding or catalytic activity. FEBS Lett. 1994 Jul 25;349(1):50-4. PMID:8045301 doi:10.1016/0014-5793(94)00637-7
- ↑ Keynan S, Habgood NT, Hooper NM, Turner AJ. Site-directed mutagenesis of conserved cysteine residues in porcine membrane dipeptidase. Cys 361 alone is involved in disulfide-linked dimerization. Biochemistry. 1996 Sep 24;35(38):12511-7. PMID:8823187 doi:10.1021/bi961193z
