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 | Comment | Organism | GeneOntology No. | Textmining |
---|
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
150000 | - |
fusion protein | Leishmania major |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leishmania major | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + dihydroxyacetone phosphate | - |
Leishmania major | CoA + acyldihydroxyacetone phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LmDAT | - |
Leishmania major |
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 |