Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.42 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)

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

Protein Variants

Protein Variants Comment Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Leishmania major
-
V1
-
Leishmania major V1
-
V1
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DHAPAT
-
Leishmania major
dihydroxyacetonephosphate acyltransferase
-
Leishmania major
LmDAT
-
Leishmania major

General Information

General Information Comment Organism
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
metabolism catalyses initial step for glycerolipid metabolism, such as ether lipid derived virulence factor lipophosphoglycan and glycosylphosphatidylinositol-anchored proteins Leishmania major
physiological function important for normal growth, survival during stationary phase, and virulence Leishmania major