Ontology highlight
ABSTRACT:
SUBMITTER: Steinhauer J
PROVIDER: S-EPMC2793297 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Steinhauer Josefa J Gijón Miguel A MA Riekhof Wayne R WR Voelker Dennis R DR Murphy Robert C RC Treisman Jessica E JE
Molecular biology of the cell 20091201 24
Enzymes of the membrane-bound O-acyltransferase (MBOAT) family add fatty acyl chains to a diverse range of protein and lipid substrates. A chromosomal translocation disrupting human MBOAT1 results in a novel syndrome characterized by male sterility and brachydactyly. We have found that the Drosophila homologues of MBOAT1, Oysgedart (Oys), Nessy (Nes), and Farjavit (Frj), are lysophospholipid acyltransferases. When expressed in yeast, these MBOATs esterify specific lysophospholipids preferentiall ...[more]