MBOAT2

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 sequence, conserved histidine (His) embedded in a hydrophobic stretch of amino-acid, residues and an asparagine (Asn) or histidine within a more hydrophilic region some 30-50 residues upstream.

MBOAT enzymes catalyze the transfer of an acyl group from an Acyl-coenzyme A, acyl-coenzyme or accessory protein to one of several different Substrate (biochemistry), substrates. The family is found from bacteria to eukaryotes.

The family may be grouped into three categories, according to function:
#enzymes involved in neutral Lipid synthesis, lipid biosynthesis;
#enzymes involved in protein/peptide acylation;
#enzymes involved in phospholipid re-modelling.

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. A computational model of human Ghrelin O-acyltransferase, ghrelin ''O''-acyltransferase (GOAT)
Q96T53
revealed a transmembrane channel that facilitates octanoylation of the peptide hormone ghrelin. 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

Enzymes
Membrane proteins
Protein families