PRDX6 gene

The HOXA1 gene (HOXA1 stands for: Homeobox A1) is a protein-coding gene located on chromosome 7p15.2. Two transcript variants encoding two different isoforms have been found for this gene, with only one of the isoforms containing the homeodomain region. An important paralog of this gene is HOXB1.

The protein encoded by this gene belongs to the family of thiol-specific antioxidant proteins. This protein is a bifunctional enzyme with two different active sites. It is involved in the redox regulation of the cell; it can reduce H(2)O(2) and short-chain organic, fatty acid and phospholipid hydroperoxides. It may play a role in regulating phospholipid turnover and protecting against oxidative damage. [provided by RefSeq, Jul 2008]

The PRDX6 gene encodes a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Kang SW et al. 1998; Chen JW et al. 2000). Can reduce H(2)O(2) and short-chain organic, fatty acid and phospholipid hydroperoxides (Chen JW et al. 2000). The encoded thiol-specific peroxidase also has phospholipase activity, so it can either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (Fisher AB et al. 2016). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipids at cytosolic pH ((Chen JW et al. 2000). Peroxidase plays a role in cell protection against oxidative stress by detoxification of peroxides and in phospholipid homeostasis. It has an acyl-CoA-dependent lysophospholipid acyltransferase that mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC).

1. Chen JW et al. (2000) 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J Biol Chem 275:28421-28427.
2. Fisher AB et al. (2016) A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6. J Lipid Res 57:587-596.
3. Kang SW et al. (1998) Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J Biol Chem 273:6303-6311