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Literature summary for 2.3.1.23 extracted from

  • Lin, S.; Ikegami, M.; Moon, C.; Naren, A.P.; Shannon, J.M.
    Lysophosphatidylcholine acyltransferase 1 (LPCAT1) specifically interacts with phospholipid transfer protein starD10 to facilitate surfactant phospholipid trafficking in alveolar type II cells (2015), J. Biol. Chem., 290, 18559-18574.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene LPCAT1, recombinant expression of FLAG- and HA-tagged full-length and truncated enzyme in HEK-293 cell microsomes, recombinant coexpression of His-tagged or GST-tagged enzyme with His-tagged StarD10 protein in Escherichia coli Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Mus musculus 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine Mus musculus
-
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine Mus musculus FVB/N
-
CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
additional information Mus musculus enzyme LPCAT1 directly interacts with StarD10 protein, amino acids 79-271 of LPCAT1 and the steroidogenic acute regulatory protein-related lipid transfer (START) domain of START domain-containing protein 10 (StarD10) are sufficient for this interaction. The enzyme also interacts with StarD7-I but not StarD7-II or StarD2/PCTP transfer protein ?
-
?
additional information Mus musculus FVB/N enzyme LPCAT1 directly interacts with StarD10 protein, amino acids 79-271 of LPCAT1 and the steroidogenic acute regulatory protein-related lipid transfer (START) domain of START domain-containing protein 10 (StarD10) are sufficient for this interaction. The enzyme also interacts with StarD7-I but not StarD7-II or StarD2/PCTP transfer protein ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus Q3TFD2
-
-
Mus musculus FVB/N Q3TFD2
-
-

Purification (Commentary)

Purification (Comment) Organism
copurification of His-tagged or GST-tagged enzyme with His-tagged StarD10 protein from Escherichia coli by affinity chromatography Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
alveolar type II cell
-
Mus musculus
-
epithelial cell
-
Mus musculus
-
liver
-
Mus musculus
-
lung
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
-
Mus musculus CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine specificity of enzyme LPCAT1 for lyso-PC as an acyl acceptor Mus musculus CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
-
Mus musculus FVB/N CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine specificity of enzyme LPCAT1 for lyso-PC as an acyl acceptor Mus musculus FVB/N CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
?
additional information enzyme LPCAT1 directly interacts with StarD10 protein, amino acids 79-271 of LPCAT1 and the steroidogenic acute regulatory protein-related lipid transfer (START) domain of START domain-containing protein 10 (StarD10) are sufficient for this interaction. The enzyme also interacts with StarD7-I but not StarD7-II or StarD2/PCTP transfer protein Mus musculus ?
-
?
additional information enzyme LPCAT1 directly interacts with StarD10 protein, amino acids 79-271 of LPCAT1 and the steroidogenic acute regulatory protein-related lipid transfer (START) domain of START domain-containing protein 10 (StarD10) are sufficient for this interaction. The enzyme also interacts with StarD7-I but not StarD7-II or StarD2/PCTP transfer protein Mus musculus FVB/N ?
-
?

Synonyms

Synonyms Comment Organism
LPCAT1
-
Mus musculus
lyso-PC acyltransferase 1
-
Mus musculus
lysophosphatidylcholine acyltransferase 1
-
Mus musculus

General Information

General Information Comment Organism
physiological function pulmonary surfactant, a mixture of proteins and phospholipids, plays an important role in facilitating gas exchange by maintaining alveolar stability. Saturated phosphatidylcholine, the major component of surfactant, is synthesized both de novo and by the remodeling of unsaturated phosphatidylcholine by lyso-PC acyltransferase 1 (LPCAT1). After synthesis in the endoplasmic reticulum, saturated phosphatidylcholine is routed to lamellar bodies for storage prior to secretion. The enzyme forms a transient complex with saturated phosphatidylcholine and specific phospholipid transport protein(s) to initiate trafficking of saturated phosphatidylcholine from the endoplasmic reticulum to the lamellar bodies Mus musculus