AGPAT8 has moderate acyltransferase activity, only 18.4% when compared to the other isoform, AGPAT2, using oleoyl-CoA as the acyl donor and 1-oleoyl-3-phosphate-glycerol as the acceptor
overexpression shows 1-acyl-sn-glycero-3-phosphate acyltransferase activity but no lysophosphatidylcholine acyltransferase activity, acyl-CoA specificity and specificity of lysophosphatidic acids (LPAs) listed, substitution of asparagine with proline in the NHX4D motif and arginine with cysteine in the EGTR motif, mutant retains enzyme activity, model proposed in which a hydrophobic pocket in 1-acyl-sn-glycero-3-phosphate acyltransferase 9 accommodates fatty acyl chains of both substrates in proper orientation, whereas the HX4D motif participates in catalysis
overexpression shows 1-acyl-sn-glycero-3-phosphate acyltransferase activity but no lysophosphatidylcholine acyltransferase activity, acyl-CoA specificity and specificity of lysophosphatidic acids (LPAs) listed, substitution of asparagine with proline in the NHX4D motif and arginine with cysteine in the EGTR motif, mutant retains enzyme activity, model proposed in which a hydrophobic pocket in 1-acyl-sn-glycero-3-phosphate acyltransferase 9 accommodates fatty acyl chains of both substrates in proper orientation, whereas the HX4D motif participates in catalysis
topology of motifs I and III confirmed by experiments with recombinant AGPAT1, catalytic roles of highly conserved residues in the four acyltransferase motifs analyzed by site-directed mutagenesis, sidechain modification of His104, Asp109, Phe146, Arg149, Glu178, Gly179, Thr180, Arg181 and Ile208 shows motif importance for catalysis, substrate accessibility to the catalytic domain analyzed by competition assay, catalytic domain not accessed by lysophosphatidic acid (LPA) with fatty acid chains shorter than 10 carbons, hydrophobicity of lysophosphatidic acid important, catalytic domain accessed by short chain acyl-CoAs but not as second substrate, motifs II and III involved in binding of lysophosphatidic acid, motifs I and IV involved in binding of acyl-CoA
topology of motifs I and III confirmed by experiments with recombinant AGPAT1, catalytic roles of highly conserved residues in the four acyltransferase motifs analyzed by site-directed mutagenesis, sidechain modification of His104, Asp109, Phe146, Arg149, Glu178, Gly179, Thr180, Arg181 and Ile208 shows motif importance for catalysis, substrate accessibility to the catalytic domain analyzed by competition assay, catalytic domain not accessed by lysophosphatidic acid (LPA) with fatty acid chains shorter than 10 carbons, hydrophobicity of lysophosphatidic acid important, catalytic domain accessed by short chain acyl-CoAs but not as second substrate, motifs II and III involved in binding of lysophosphatidic acid, motifs I and IV involved in binding of acyl-CoA
absence of transmembrane domains, presence of hydrolase/acyltransferase domain with a distinct lipid-binding motif and a lysophospholipase domain, reduced phosphatidic acid in mutants suggests a role in phosphatidic acid biosynthesis, overexpression shows increase in phosphatidic acid and other phospholipids on organic solvent exposure, recombinant protein acylates lysophosphatidic acid, substrate preference analyzed, nearly no activity with lysophospholipids such as lysophosphatidylcholine (LPC), lysophosphatidylethanolamine (LPE), and lysophosphatidylserine (LPS)
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids
deletion of Slc1p alone not lethal, microsomal enzyme activity not completely lost, evidence for additional enzyme activity, comparison between Slc1p with Slc4p, single mutants of Slc1p and Slc4p generated, double mutant of Slc1p and Slc4p lethal, same glycerophospholipid profiles but different lipid profiles between Slc1p and Slc4p, both enzymes able to use endogenous lysoglycerophospholipids as substrates, substrate specificity between Slc1p and Slc4p different or access to different lysoglycerophospholipid substrates because of a different subcellular location, Slc1p and Slc4p are both active as acyltransferases and are also involved in fatty acid exchange at the sn-2-position of mature glycerophospholipids
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location
microsomal enzyme activity not completely lost by deletion of Slc1p, evidence for additional enzyme activity, SLC4 gene encodes second enzmye indicated by lethality of double mutants of Slc1p and Slc4p, same glycerophospholipid profile but different lipid profiles between Slc1p and Slc4p, different substrate specificity between Slc1p and Slc4p or access to different lysoglycerophospholipid substrates because of a different subcellular location