Ca+2-independent phospholipase-A2 (peroxiredoxin 6, PRDX6, antioxidant protein 2, 1-Cys peroxiredoxin, 1-Cys PRX, acidic calcium-independent phospholipase A2, aiPLA2, non-selenium glutathione peroxidase, NSGPx, 24 kDa protein, liver 2D page spot 40, red blood cells page spot 12)
Jump to navigation
Jump to search
Function
- role in redox regulation of the cell
- can reduce H2O2 & short chain organic, fatty acid, & phospholipid hydroperoxides
- may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury
- may interact with HTR2A (putative)
- interacts with STH
- active site is the redox-active cys-47 oxidized to cys-SOH
- cys-SOH may rapidly react with a cys-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation
- enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin
2 R'-SH + ROOH <--> R'-S-S-R' + H2O + ROH
Donor + H2O2 <--> oxidized donor + 2 H2O
Structure
- homotetramer
- belongs to the ahpC/TSA family. Rehydrin subfamily
Compartment
- cytoplasm (putative), lysosome
- cytoplasmic vesicle (putative)
- found in lung secretory organelles (putative)
Expression
- bound in virtually all organs with largest amounts in brain, lung, heart, & liver
Pathology
- irreversibly inactivated by overoxidation of cys-47 (to cys-SO(3)H) upon oxidative stress
More general terms
References
- ↑ Mayer RJ, Marshall LA. New insights on mammalian phospholipase A2(s); comparison of arachidonoyl-selective and -nonselective enzymes. FASEB J. 1993 Feb 1;7(2):339-48. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8440410
- ↑ UniProt http://www.uniprot.org/uniprot/P30041.html