{
    "title": "Ether lipid biosynthesis: alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities.",
    "journal": "Journal of lipid research",
    "date": "1999",
    "authors": "de Vet EC, Ijlst L, Oostheim W, Dekker C, Moser HW, van Den Bosch H, Wanders RJ",
    "reference": {
        "type": "PubMed",
        "id": "10553003",
        "url": "https://pubmed.ncbi.nlm.nih.gov/10553003"
    },
    "referenced_proteins": [
        "Q9BZM1-1",
        "Q6NUI2-1",
        "P04054-1",
        "P09923-1",
        "P43304-1",
        "Q8N335-1",
        "Q8NEL9-1",
        "Q53EU6-1",
        "Q7L4E1-1",
        "Q86XP0-1",
        "Q6XZB0-1",
        "O94830-1",
        "P0C869-1",
        "Q8NAN2-1",
        "Q9NPH0-1",
        "Q13393-1",
        "Q99943-1",
        "Q86UL3-1",
        "Q9UNK4-1",
        "Q9NRZ7-1",
        "Q6UWP7-1",
        "O15120-1",
        "O14939-1",
        "Q8N2A8-1",
        "Q9NUQ2-1",
        "P14555-1",
        "Q9NRZ5-1",
        "Q8NF37-1",
        "Q8WWY8-1",
        "P39877-1",
        "Q9NZK7-1",
        "Q13018-1",
        "P47712-1",
        "P21695-1",
        "Q643R3-1",
        "O15496-1",
        "Q9HCL2-1",
        "Q9BZM2-1",
        "O15228-1"
    ],
    "referenced_glycans": [],
    "species": [
        {
            "name": "Homo sapiens",
            "taxid": 9606,
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "Q9BZM1",
                    "url": "https://www.uniprot.org/uniprot/Q9BZM1"
                }
            ],
            "common_name": "Human"
        }
    ],
    "record_id": "pubmed.10553003",
    "abstract": "Recent studies have indicated that two peroxisomal enzymes involved in ether lipid synthesis, i.e., dihydroxyacetonephosphate acyltransferase and alkyl-dihydroxyacetonephosphate synthase, are directed to peroxisomes by different targeting signals, i.e., peroxisomal targeting signal type 1 and type 2, respectively. In this study, we describe a new human fibroblast cell line in which alkyl-dihydroxyacetonephosphate synthase was found to be deficient both at the level of enzyme activity and enzyme protein. At the cDNA level, a 128 base pair deletion was found leading to a premature stop. Remarkably, dihydroxyacetonephosphate acyltransferase activity was strongly reduced to a level comparable to the activities measured in fibroblasts from patients affected by the classical form of rhizomelic chondrodysplasia punctata (caused by a defect in peroxisomal targeting signal type 2 import). Dihydroxyacetonephosphate acyltransferase activity was completely normal in another alkyl-dihydroxyacetonephosphate synthase activity-deficient patient. Fibroblasts from this patient showed normal levels of the synthase protein and inactivity results from a point mutation leading to an amino acid substitution. These results strongly suggest that the activity of dihydroxyacetonephosphate acyltransferase is dependent on the presence of alkyl-dihydroxyacetonephosphate synthase protein. This interpretation implies that the deficiency of dihydroxyacetonephosphate acyltransferase (targeted by a peroxisomal targeting signal type 1) in the classic form of rhizomelic chondrodysplasia punctata is a consequence of the absence of the alkyl-dihydroxyacetonephosphate synthase protein (targeted by a peroxisomal targeting signal type 2).",
    "glycosylation": [],
    "mutagenesis": [],
    "snv": [],
    "phosphorylation": [],
    "glycation": []
}