[1] MBOAT enzymes catalyze the transfer of an acyl group from an acyl-coenzyme or accessory protein to one of several different substrates.
[2] The family may be grouped into three categories, according to function: The structure for one MBOAT protein, DltB from Streptococcus thermophilus (Q5M4V4), has been solved.
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.
[5] DltB and GOAT share structural similarities in their homologous regions, suggesting a common core fold for MBOAT family members.