MBOAT
| MBOAT | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | MBOAT | ||||||||
| Pfam | PF03062 | ||||||||
| Pfam clan | CL0517 | ||||||||
| InterPro | IPR004299 | ||||||||
| |||||||||
| MBOAT_2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | MBOAT_2 | ||||||||
| Pfam | PF13813 | ||||||||
| Pfam clan | CL0517 | ||||||||
| InterPro | IPR004299 | ||||||||
| |||||||||
The MBOAT (membrane bound O-acyl transferase) family of membrane proteins is a family of various acyltransferase enzymes. All family members contain multiple transmembrane domains and most carry two conserved residues which might be active-site residues, a conserved histidine (His) embedded in a hydrophobic stretch of residues and an asparagine (Asn) or histidine within a more hydrophilic region some 30-50 residues upstream.[1]
MBOAT enzymes catalyze the transfer of an acyl group from acyl-coenzyme to one of several different substrates. The family is found from bacteria to eukaryotes, and the active region lies outside the membrane.[2]
The family may be grouped into four categories, according to function:
- Subgroup 1: enzymes involved in neutral lipid biosynthesis;
- Subgroup 2: enzymes involved in protein/peptide acylation;
- Subgroup 3: enzymes involved in phospholipid re-modelling.[3]
References
- ↑ Hofmann K (March 2000). "A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling". Trends Biochem. Sci. 25 (3): 111–2. PMID 10694878. doi:10.1016/s0968-0004(99)01539-x.
- ↑ Schmoldt A, Benthe HF, Haberland G (1975). "Digitoxin metabolism by rat liver microsomes.". Biochem Pharmacol. 24 (17): 1639–41. PMID 10. doi:10.1016/0006-2952(75)90094-5.
- ↑ Wang P, Wang Z, Dou Y, Zhang X, Wang M, Tian X (2013). "Genome-wide identification and analysis of membrane-bound O-acyltransferase (MBOAT) gene family in plants.". Planta. 238 (5): 907–22. PMID 23928653. doi:10.1007/s00425-013-1939-4.
- Chang CCY, Sun J, Chang TY. Membrane-bound O-acyltransfereses (MBOATs). Front. Biol. 6(3), 177-182 (2011)
This article incorporates text from the public domain Pfam and InterPro IPR004299