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Localization of the initial steps in alkoxyphospholipid biosynthesis in glycosomes (microbodies) of Trypanosoma brucei
Author(s) -
Opperdoes Fred R.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80284-7
Subject(s) - trypanosoma brucei , microbody , acyltransferase , biochemistry , dihydroxyacetone phosphate , dhap , acyltransferases , glycerol , biosynthesis , organelle , enzyme , reductase , biology , peroxisome , chemistry , gene , catalase
Cell fractionation of Trypanosoma brucei cultured procyclic stages showed that the key enzyme of glycerol‐ether lipid synthesis, dihydroxycetone‐phosphate acyltransferase (EC 2.3.1.42) was exclusively associated with the microbody fraction. These organelles contained in addition 1‐acyl glycerol‐3‐phosphate:NADP + oxidoreductase (EC 1.1.1.101) and acyl‐CoA reductase and were capable of utilizing DHAP, but not G‐3‐P, as substrate for lysophosphatidic acid formation. It is concluded that in T. brucei the glycosomes are the exclusive site of the synthesis of precursors for glycerol‐ether lipid synthesis and that they contain the entire pathway to form alkoxylipids from glycerol and acyl‐CoA.