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 conservedhistidine (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]
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.
^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.
^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.
^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. PMC6768652. PMID 31413115.
This article incorporates text from the public domain Pfam and InterPro: IPR004299
April 18, 2024
mboat, membrane, bound, acyl, transferase, family, membrane, proteins, family, various, acyltransferase, enzymes, family, members, contain, multiple, transmembrane, domains, most, carry, conserved, residues, conserved, histidine, embedded, hydrophobic, stretch. 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 MBOATIdentifiersSymbolMBOATPfamPF03062Pfam clanCL0517InterProIPR004299Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryMBOAT 2IdentifiersSymbolMBOAT 2PfamPF13813Pfam clanCL0517Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryMBOAT 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 editThe 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 editDGAT1 GUP1 HHAT HHATL LPCAT3 MBOAT1 MBOAT2 MBOAT4 MBOAT7 PORCN SOAT1 SOAT2References 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 amp Chang TY 2011 Membrane bound O acyltransferases MBOATs Front Biol 6 3 177 doi 10 1007 s11515 011 1149 z S2CID 41626991 a href Template Cite journal html title Template Cite journal cite journal a 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 Campana 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 This article incorporates text from the public domain Pfam and InterPro IPR004299 Retrieved from https en wikipedia org w index php title MBOAT amp oldid 1188302461, wikipedia, wiki, book, books, library,
