MBOAT explained
| Symbol: | MBOAT |
| MBOAT |
| Pfam: | PF03062 |
| Pfam Clan: | CL0517 |
| Interpro: | IPR004299 |
| Symbol: | MBOAT_2 |
| MBOAT_2 |
| Pfam: | PF13813 |
| Pfam Clan: | CL0517 |
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, 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 an acyl-coenzyme or accessory protein to one of several different substrates. The family is found from bacteria to eukaryotes.[2]
The family may be grouped into three categories, according to function:
- enzymes involved in neutral lipid biosynthesis;
- enzymes involved in protein/peptide acylation;
- enzymes involved in phospholipid re-modelling.[3]
Structure
The structure for one MBOAT protein, DltB from Streptococcus thermophilus, has been solved. DltB performs D-alanylation of cell-wall teichoic acid. It contains a ring of 11 transmembrane helices surrounding a tunnel that goes through the biological membrane. The tunnel connects to a partner, DltC, which carries the D-alanine to the conserved histidine residue of DltB MBOAT located at the bottom of the funnel.[4] A computational model of human ghrelin O-acyltransferase (GOAT) (Q96T53) revealed a transmembrane channel that facilitates octanoylation of the peptide hormone ghrelin.[5] DltB and GOAT share structural similarities in their homologous regions, suggesting a common core fold for MBOAT family members.
Notes and References
- Hofmann K . A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling . Trends Biochem. Sci. . 25 . 3 . 111–2 . March 2000 . 10694878 . 10.1016/s0968-0004(99)01539-x.
- Chang, C.C.Y., Sun, J. & Chang, TY.. 2011. Membrane-bound O-acyltransferases (MBOATs). Front. Biol.. 6. 3. 177. 10.1007/s11515-011-1149-z. 41626991.
- Wang P, Wang Z, Dou Y, Zhang X, Wang M, Tian X. Genome-wide identification and analysis of membrane-bound O-acyltransferase (MBOAT) gene family in plants. . Planta . 2013 . 238 . 5 . 907–22 . 23928653 . 10.1007/s00425-013-1939-4 . 2013Plant.238..907W . 1328304 .
- Ma . D . Wang . Z . Merrikh . CN . Lang . KS . Lu . P . Li . X . Merrikh . H . Rao . Z . Xu . W . Crystal structure of a membrane-bound O-acyltransferase. . Nature . October 2018 . 562 . 7726 . 286–290 . 10.1038/s41586-018-0568-2 . 30283133 . 6529733. 2018Natur.562..286M .
- Campaña. Maria B.. Irudayanathan. Flaviyan Jerome. Davis. Tasha R.. McGovern-Gooch. Kayleigh R.. Loftus. Rosemary. Ashkar. Mohammad. Escoffery. Najae. Navarro. Melissa. Sieburg. Michelle A.. Nangia. Shikha. Hougland. James L.. 27 September 2019. The ghrelin O-acyltransferase structure reveals a catalytic channel for transmembrane hormone acylation. The Journal of Biological Chemistry. 294. 39. 14166–14174. 10.1074/jbc.AC119.009749. 1083-351X. 6768652. 31413115. free.
