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Literature summary extracted from

  • Zufferey, R.; Al-Ani, G.K.; Dunlap, K.
    Leishmania dihydroxyacetonephosphate acyltransferase LmDAT is important for ether lipid biosynthesis but not for the integrity of detergent resistant membranes (2009), Mol. Biochem. Parasitol., 168, 177-185.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.42 PCR-amplification, transfection of Leishmania by electroporation Leishmania major

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.42 additional information null mutant deltalmdat/deltalmdat, and complemented null mutant, double mutants with additional loss of glycerol-3-phosphate acyltransferase (LmGAT) are not viable, thus, these two may be the only acyltransferases Leishmania major

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.42 glycosome
-
 Leishmania major 20015
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.42 dihydroxyacetone phosphate + acyl-CoA Leishmania major
-
 1-acyl-glycerone phosphate + CoA
-
 ?
2.3.1.42 dihydroxyacetone phosphate + acyl-CoA Leishmania major V1
-
 1-acyl-glycerone phosphate + CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.42 Leishmania major
-
 V1
-
2.3.1.42 Leishmania major V1
-
 V1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.42 dihydroxyacetone phosphate + acyl-CoA
-
 Leishmania major 1-acyl-glycerone phosphate + CoA
-
 ?
2.3.1.42 dihydroxyacetone phosphate + acyl-CoA
-
 Leishmania major V1 1-acyl-glycerone phosphate + CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.42 DHAPAT
-
 Leishmania major
2.3.1.42 dihydroxyacetonephosphate acyltransferase
-
 Leishmania major
2.3.1.42 LmDAT
-
 Leishmania major

General Information

EC Number General Information Comment Organism
2.3.1.42 malfunction null mutant produces longer lipophosphoglycan molecules, that migrate slower into the membrane and are not released into the medium, levels of glycosylphosphatidylinositol-anchored proteins are increased in the membrane (maybe due to slower trnasperot through the secretory pathway), however, the integrity of detergent resistant membranes is not affected, and the typical metacyclic genes such as SHERP are still expressed, arabinosylated forms of lipophosphoglycan are still produced, and the normal morphology is still exhibited Leishmania major
2.3.1.42 metabolism catalyses initial step for glycerolipid metabolism, such as ether lipid derived virulence factor lipophosphoglycan and glycosylphosphatidylinositol-anchored proteins Leishmania major
2.3.1.42 physiological function important for normal growth, survival during stationary phase, and virulence Leishmania major