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Literature summary for 2.3.1.42 extracted from

  • Al-Ani, G.; Patel, N.; Pirani, K.; Zhu, T.; Dhalladoo, S.; Zufferey, R.
    The N-terminal domain and glycosomal localization of Leishmania initial acyltransferase LmDAT are important for lipophosphoglycan synthesis (2011), PLoS ONE, 6, e27802.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K852L mutant shows no activity and fails to support normal growth and survival during the stationary phase Leishmania major
additional information deletion analyses show that the large N-terminal extension of this initial acyltransferase may be important for its stability or activity. Abrogation of the C-terminal glycosomal targeting signal sequence of LmDAT lead to extraglycosomal localization, do not impair its enzymatic activity but affect synthesis of the ether glycerolipid-based virulence factor lipophosphoglycan Leishmania major

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
fusion protein Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
LmDAT
-
Leishmania major

General Information

General Information Comment Organism
malfunction an active enzyme is critical for normal growth and survival during the stationary phase. Deletion analyses show that the large N-terminal extension of this initial acyltransferase may be important for its stability or activity. Abrogation of the C-terminal glycosomal targeting signal sequence of LmDAT lead to extraglycosomal localization, do not impair its enzymatic activity but affect synthesis of the ether glycerolipid-based virulence factor lipophosphoglycan Leishmania major