Reactome | palmitoyl-CoA + DHAP => 1-palmitoylglycerone phosphate + CoASH

palmitoyl-CoA + DHAP => 1-palmitoylglycerone phosphate + CoASH

Stable Identifier

R-HSA-75879

Type

Reaction [transition]

Species

Homo sapiens

Compartment

peroxisomal matrix

ReviewStatus

5/5

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palmitoyl-CoA + DHAP => 1-palmitoylglycerone phosphate + CoASH

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Peroxisomal glyceronephosphate O-acyltransferase (GNPAT) catalyzes the reaction of palmitoyl-CoA and DHAP to form 1-palmitoyl glycerone phosphate (1-palmitoyl dihydroxyacetone phosphate) and CoASH. The active form of the enzyme is one subunit of a heterotrimer with two molecules of the alkylglycerone phosphate synthase (AGPS) enzyme (Biermann et al. 1999). It was first purified and characterized biochemically by Ofman and Wanders (1994). Mutations in the GNPAT gene are associated with rhizomelic chondrodysplasia type 2 (Ofman et al. 1998, 2001).

Literature References

PubMed ID	Title	Journal	Year
10215861	Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes Biermann, J, Just, WW, van den Bosch, H, Wanders, RJA	Eur J Biochem	1999
8186247	Purification of peroxisomal acyl-CoA: dihydroxyacetonephosphate acyltransferase from human placenta Wanders, RJA, Ofman, R	Biochim Biophys Acta	1994
9536089	Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2 Hogenhout, EM, Muijsers, AO, Wanders, RJA, Caruso, U, Hettema, EH, Ofman, R	Hum Mol Genet	1998
11237722	Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations Lajmir, S, Wanders, RJA, Ofman, R	Biochem Biophys Res Commun	2001