LMPD Database

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LMP007254

UniProt Annotations

Entry Information
Gene NameAle1p
Protein EntryALE1_YEAST
UniProt IDQ08548
SpeciesYeast (S288c)
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=10 uM for oleoyl-CoA (with lysophosphoethanolamine as cosubstrate); KM=17 uM for palmitoleoyl-CoA (with lysophosphoethanolamine as cosubstrate); KM=0.9 uM for palmitoyl-CoA (with lysophosphoethanolamine as cosubstrate); KM=0.4 uM for myristoyl-CoA (with lysophosphoethanolamine as cosubstrate); KM=49 uM for oleoyl-CoA (with lysophosphocholine as cosubstrate); KM=21 uM for palmitoleoyl-CoA (with lysophosphocholine as cosubstrate); KM=1.8 uM for palmitoyl-CoA (with lysophosphocholine as cosubstrate); KM=5.9 uM for stearoyl-CoA (with lysophosphocholine as cosubstrate); KM=11 uM for arachidonyl-CoA (with lysophosphocholine as cosubstrate); Vmax=38 nmol/min/mg enzyme with oleoyl-CoA as substrate (with lysophosphoethanolamine as cosubstrate); Vmax=44 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with lysophosphoethanolamine as substrate); Vmax=3.7 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with lysophosphoethanolamine as substrate); Vmax=1.2 nmol/min/mg enzyme with myristoyl-CoA as substrate (with lysophosphoethanolamine as substrate); Vmax=125 nmol/min/mg enzyme with oleoyl-CoA as substrate (with lysophosphocholine as substrate); Vmax=142 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with lysophosphocholine as substrate); Vmax=7.8 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with lysophosphocholine as substrate); Vmax=12 nmol/min/mg enzyme with stearoyl-CoA as substrate (with lysophosphocholine as substrate); Vmax=58 nmol/min/mg enzyme with arachidonyl-CoA as substrate (with lysophosphocholine as substrate); pH dependence: Optimum pH is 6.5-7.5.;
Catalytic ActivityAcyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
Catalytic ActivityAcyl-CoA + 1-acyl-sn-glycero-3- phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3- phosphoethanolamine.
Catalytic ActivityAcyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
FunctionMembrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids. Preferentially acylates lysophosphocholine, but also lysophosphoethanolamine and lysophosphatidylglycerol. {ECO:0000269|PubMed:17652094, ECO:0000269|PubMed:17675291, ECO:0000269|PubMed:17726007, ECO:0000269|PubMed:17996202}.
SimilarityBelongs to the membrane-bound acyltransferase family. {ECO:0000305}.
Subcellular LocationEndoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein.