IPR022270
Beta-carotene 15,15'-dioxygenase, Brp/Blh family
InterPro entry
Short name | Blh_diox |
Description
This prokaryotic integral membrane protein family includes Brp (bacterio-opsin related protein) and Blh (Brp-like protein). Bacteriorhodopsin is a light-driven proton pump consisting of the membrane apoprotein bacterioopsin and a covalently bound retinal cofactor that appears to be derived of beta-carotene. Blh has been shown to cleave beta-carotene
[1] to produce two all-trans retinal molecules. It has been suggested that Brp and Blh are similar proteins that catalyze or regulate the conversion of beta-carotene to retinal
[2]. Mammalian enzymes with similar enzymatic function are not multiple membrane spanning proteins and are not homologous.
References
1.In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a beta-carotene 15,15'-dioxygenase. Kim YS, Kim NH, Yeom SJ, Kim SW, Oh DK. J. Biol. Chem. 284, 15781-93, (2009). View articlePMID: 19366683
2.brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum. Peck RF, Echavarri-Erasun C, Johnson EA, Ng WV, Kennedy SP, Hood L, DasSarma S, Krebs MP. J. Biol. Chem. 276, 5739-44, (2001). View articlePMID: 11092896
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME