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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | MBOAT | ||||||||
| Pfam | PF03062 | ||||||||
| Pfam clan | CL0517 | ||||||||
| InterPro | IPR004299 | ||||||||
| |||||||||
| MBOAT_2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | MBOAT_2 | ||||||||
| Pfam | PF13813 | ||||||||
| Pfam clan | CL0517 | ||||||||
| |||||||||
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 edit
The structure for one MBOAT protein, DltB from Streptococcus thermophilus (Q5M4V4), 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.
Human proteins with this domain edit
References edit
- ^ Hofmann K (March 2000). "A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling". Trends Biochem. Sci. 25 (3): 111–2. doi:10.1016/s0968-0004(99)01539-x. PMID 10694878.
- ^ Chang, C.C.Y., Sun, J. & Chang, TY. (2011). "Membrane-bound O-acyltransferases (MBOATs)". Front. Biol. 6 (3): 177. doi:10.1007/s11515-011-1149-z. S2CID 41626991.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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. Bibcode:2013Plant.238..907W. doi:10.1007/s00425-013-1939-4. PMID 23928653. S2CID 1328304.
- ^ Ma, D; Wang, Z; Merrikh, CN; Lang, KS; Lu, P; Li, X; Merrikh, H; Rao, Z; Xu, W (October 2018). "Crystal structure of a membrane-bound O-acyltransferase". Nature. 562 (7726): 286–290. Bibcode:2018Natur.562..286M. doi:10.1038/s41586-018-0568-2. PMC 6529733. PMID 30283133.
- ^ 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. doi:10.1074/jbc.AC119.009749. ISSN 1083-351X. PMC 6768652. PMID 31413115.