mBOAT
{{Short description|Family of various acyltransferase enzymes}}
{{Infobox protein family
| Symbol = MBOAT
| Name = MBOAT
| image =
| width =
| caption =
| Pfam = PF03062
| Pfam_clan = CL0517
| InterPro = IPR004299
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = MBOAT_2
| Name = MBOAT_2
| image =
| width =
| caption =
| Pfam = PF13813
| Pfam_clan = CL0517
| InterPro =
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
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.{{cite journal | author = Hofmann K | title = A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling | journal = Trends Biochem. Sci. | volume = 25 | issue = 3 | pages = 111–2 |date=March 2000 | pmid = 10694878 | doi = 10.1016/s0968-0004(99)01539-x}}
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.{{Cite journal|last=Chang, C.C.Y., Sun, J. & Chang, TY.|date=2011|title=Membrane-bound O-acyltransferases (MBOATs)|journal=Front. Biol.|volume=6|issue=3|pages=177|doi=10.1007/s11515-011-1149-z|s2cid=41626991}}
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.{{cite journal| vauthors =Wang P, Wang Z, Dou Y, Zhang X, Wang M, Tian X| title=Genome-wide identification and analysis of membrane-bound O-acyltransferase (MBOAT) gene family in plants. | journal=Planta | year= 2013 | volume= 238 | issue= 5 | pages= 907–22 | pmid=23928653 | doi=10.1007/s00425-013-1939-4 | bibcode=2013Plant.238..907W | s2cid=1328304 }}
Structure
The structure for one MBOAT protein, DltB from Streptococcus thermophilus ({{PDBe-KB|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.{{cite journal |last1=Ma |first1=D |last2=Wang |first2=Z |last3=Merrikh |first3=CN |last4=Lang |first4=KS |last5=Lu |first5=P |last6=Li |first6=X |last7=Merrikh |first7=H |last8=Rao |first8=Z |last9=Xu |first9=W |title=Crystal structure of a membrane-bound O-acyltransferase. |journal=Nature |date=October 2018 |volume=562 |issue=7726 |pages=286–290 |doi=10.1038/s41586-018-0568-2 |pmid=30283133 |pmc=6529733|bibcode=2018Natur.562..286M }} A computational model of human ghrelin O-acyltransferase (GOAT) ([https://www.uniprot.org/uniprot/Q96T53 Q96T53]) revealed a transmembrane channel that facilitates octanoylation of the peptide hormone ghrelin.{{Cite journal|last1=Campaña|first1=Maria B.|last2=Irudayanathan|first2=Flaviyan Jerome|last3=Davis|first3=Tasha R.|last4=McGovern-Gooch|first4=Kayleigh R.|last5=Loftus|first5=Rosemary|last6=Ashkar|first6=Mohammad|last7=Escoffery|first7=Najae|last8=Navarro|first8=Melissa|last9=Sieburg|first9=Michelle A.|last10=Nangia|first10=Shikha|last11=Hougland|first11=James L.|date=27 September 2019|title=The ghrelin O-acyltransferase structure reveals a catalytic channel for transmembrane hormone acylation|journal=The Journal of Biological Chemistry|volume=294|issue=39|pages=14166–14174|doi=10.1074/jbc.AC119.009749|issn=1083-351X|pmc=6768652|pmid=31413115|doi-access=free}} DltB and GOAT share structural similarities in their homologous regions, suggesting a common core fold for MBOAT family members.
Human proteins with this domain
References
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{{InterPro content|IPR004299}}