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Information on EC 2.3.1.42 - glycerone-phosphate O-acyltransferase and Organism(s) Homo sapiens
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2.3.1.42 glycerone-phosphate O-acyltransferaseIUBMB Comments
A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA.
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Word Map
- 2.3.1.42
- peroxisomal
- plasmalogens
- zellweger
-
chondrodysplasia
-
rhizomelic
- punctata
- glycerolipids
-
phytanic
- alkyl-dhap
- hemochromatosis
- adrenoleukodystrophy
-
stippling
-
cerebro-hepato-renal
-
lignoceric
- refsum
- medicine
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gnpat, dihydroxyacetone phosphate acyltransferase, dhap-at, dhapat, dihydroxyacetonephosphate acyltransferase, dhap acyltransferase, dihydroxyacetone-phosphate acyltransferase, lmdat, glyceronephosphate o-acyltransferase, dap-at, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, dihydroxyacetone phosphate
-
-
-
-
DHAPAT
dihydroxyacetone phosphate acyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:glycerone-phosphate O-acyltransferase
A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY
37257-19-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cis-9-hexadecenoyl-CoA + dihydroxyacetone phosphate
CoA + cis-9-hexadecenoyldihydroxyacetone phosphate
-
-
-
-
?
stearoyl-CoA + dihydroxyacetone phosphate
CoA + stearoyldihydroxyacetone phosphate
-
-
-
-
ir
tetradecanoyl-CoA + dihydroxyacetone phosphate
CoA + tetradecanoyldihydroxyacetone phosphate
-
i.e. myristoyl-CoA
-
-
?
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
-
-
-
?
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
-
-
-
?
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
-
-
-
ir
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
-
-
?
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
-
-
-
?
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
-
no acyl-acceptor is glycerol 3-phosphate
i.e. acylglycerone phosphate
?
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
-
-
-
?
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
-
enzyme is essential for biosynthesis of plasmalogens and nonetherlipids, the peroxisomal isozymes does not contribute to nonetherlipid biosynthesis
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
-
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
-
-
-
ir
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
best substrate
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
obligate precursor in ether lipids biosynthesis
-
ir
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
reaction in phosphatidic acid biosynthesis
-
ir
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
peroxisomal enzyme involved in ether lipid biosynthesis
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
recombinant in Saccharomyces cerevisiae cells
-
-
?
additional information
?
-
-
enzyme activity is reduced with disorders: neonatal adrenoleukodystrophy, infantile Refsum disease, and hyperpipecolic acidemia
-
-
?
additional information
?
-
-
enzyme amount is reduced by 90% in Zellweger syndrome
-
-
?
additional information
?
-
-
enzyme amount is reduced by 90% in Zellweger syndrome
-
-
?
additional information
?
-
-
patients affected with rhizomelic chondrodysplasia punctata show reduced enzyme activity due to a defect in peroxisomal targeting
-
-
?
additional information
?
-
-
patients affected with rhizomelic chondrodysplasia punctata show reduced enzyme activity due to a defect in peroxisomal targeting
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
-
-
-
?
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
-
enzyme is essential for biosynthesis of plasmalogens and nonetherlipids, the peroxisomal isozymes does not contribute to nonetherlipid biosynthesis
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
-
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
obligate precursor in ether lipids biosynthesis
-
ir
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
reaction in phosphatidic acid biosynthesis
-
ir
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
-
peroxisomal enzyme involved in ether lipid biosynthesis
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
recombinant in Saccharomyces cerevisiae cells
-
-
?
additional information
?
-
-
enzyme activity is reduced with disorders: neonatal adrenoleukodystrophy, infantile Refsum disease, and hyperpipecolic acidemia
-
-
?
additional information
?
-
-
enzyme amount is reduced by 90% in Zellweger syndrome
-
-
?
additional information
?
-
-
enzyme amount is reduced by 90% in Zellweger syndrome
-
-
?
additional information
?
-
-
patients affected with rhizomelic chondrodysplasia punctata show reduced enzyme activity due to a defect in peroxisomal targeting
-
-
?
additional information
?
-
-
patients affected with rhizomelic chondrodysplasia punctata show reduced enzyme activity due to a defect in peroxisomal targeting
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
catalytic site at inner surface of peroxisomal membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme recruits the enzyme USP30, which deubiquitylates and stabilizes dynamin-related protein 1, thereby facilitating regulation of mitochondrial morphology, lipid metabolism, and hepatocarcinogenesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GNPAT_HUMAN
680
0
77188
Swiss-Prot
other Location (Reliability: 3)
B2RAG5_HUMAN
680
0
77307
TrEMBL
other Location (Reliability: 3)
B3KN78_HUMAN
492
0
55632
TrEMBL
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 109000, recombinant enzyme fused to enhanced green fluorescent protein, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
deficient cell line caused by DNA 128 bp deletion leading to premature stop, strongly reduced activity
additional information
-
patients affected with rhizomelic chondrodysplasia punctata show reduced enzyme activity due to a defect in peroxisomal targeting, point mutation at nucleotide 848 leading to a premature stop
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme activity and stability is dependent on alkyl-dihydroxyacetone phosphate synthase presence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose resin column chromatography, His-Trap column chromatography and Superdex S200 gel filtration
peroxisomal from placenta, with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, i.e. CHAPS, plus 1 M KCl
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme cloned from a cDNA library matching EST-clones with peptides from rabbit peroxisomal enzyme, DNA sequence determination
expression in CHO cell line NRe1-4 with severe enzyme activity defects restores the plasmalogen biosynthesis activity to 10% of wild-type activity, overexpression of the human enzyme leads to 6fold increased enzyme activity and 55% restored plasmalogen synthesizing activity, nonether glycerolipid biosynthesis is unaffected or dcreased in both cases
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
DHPAT activity is decreased in fibroblast cell lines from patients with a deficient cytosolic receptor protein PEX5
medicine
the enzyme is highly correlated with poor clinical outcome in patients with hepatocellular carcinoma
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schutgens, R.B.H.; Romeyn, G.J.; Ofman, R.; Van den Bosch, H.; Tager, J.M.; Wanders, R.J.A.
Acyl-CoA:dihydroxyacetone phosphate acyltransferase in human skin fibroblasts: study of its properties using a new assay method [published erratum appears in Biochim Biophys Acta 1987 Sep 25;921(2):415]
Biochim. Biophys. Acta
879
286-291
1986
Homo sapiens
De Vet, E.C.J.M.; Ijlst, L.; Oostheim, W.; Dekker, C.; Moser, H.W.; Van den Bosch, H.; Wanders, R.J.A.
Ether lipid biosynthesis: alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities
J. Lipid Res.
40
1998-2003
1999
Homo sapiens
Ofman, R.; Wanders, R.J.A.
Purification of peroxisomal acyl-CoA:dihydroxyacetonephosphate acyltransferase from human placenta
Biochim. Biophys. Acta
1206
27-34
1994
Homo sapiens
Thai, T.P.; Heid, H.; Rackwitz, H.R.; Hunziker, A.; Gorgas, K.; Just, W.W.
Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase
FEBS Lett.
420
205-211
1997
Homo sapiens (O15228), Homo sapiens, Oryctolagus cuniculus
Hajra, A.K.
Dihydroxyacetone phosphate acyltransferase
Biochim. Biophys. Acta
1348
27-34
1997
Saccharomyces cerevisiae, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, no activity in Schizosaccharomyces pombe, Rattus norvegicus, Saccharomyces pastorianus
Ofman, R.; Hogenhout, E.M.; Wanders, R.J.
Identification and characterization of the mouse cDNA encoding acyl-CoA:dihydroxyacetone phosphate acyltransferase
Biochim. Biophys. Acta
1439
89-94
1999
Homo sapiens (O15228), Homo sapiens, Mus musculus
Liu, D.; Nagan, N.; Just, W.W.; Rodemer, C.; Thai, T.P.; Zoeller, R.A.
Role of dihydroxyacetonephosphate acyltransferase in the biosynthesis of plasmalogens and nonether glycerolipids
J. Lipid Res.
46
727-735
2005
Cricetulus griseus, Homo sapiens
Ebberink, M.S.; Mooyer, P.A.; Koster, J.; Dekker, C.J.; Eyskens, F.J.; Dionisi-Vici, C.; Clayton, P.T.; Barth, P.G.; Wanders, R.J.; Waterham, H.R.
Genotype-phenotype correlation in PEX5-deficient peroxisome biogenesis defective cell lines
Hum. Mutat.
30
93-98
2009
Homo sapiens
Piano, V.; Nenci, S.; Magnani, F.; Aliverti, A.; Mattevi, A.
Recombinant human dihydroxyacetonephosphate acyl-transferase characterization as an integral monotopic membrane protein
Biochem. Biophys. Res. Commun.
481
51-58
2016
Homo sapiens (O15228)
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