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Information on EC 2.3.1.42 - glycerone-phosphate O-acyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q9ES71

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IUBMB Comments
A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q9ES71
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The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroxyacetone phosphate acyltransferase
-
acyltransferase, dihydroxyacetone phosphate
-
-
-
-
dihydroxyacetone phosphate acyltransferase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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 hide
37257-19-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
show the reaction diagram
acyl-CoA + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
show the reaction diagram
dihydroxyacetone phosphate + palmitoyl-CoA
palmitoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + dihydroxyacetone phosphate
CoA + dodecanoyldihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + dihydroxyacetone phosphate
CoA + oleoyldihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
show the reaction diagram
stearoyl-CoA + dihydroxyacetone phosphate
CoA + stearoyldihydroxyacetone phosphate
show the reaction diagram
tetradecanoyl-CoA + dihydroxyacetone phosphate
CoA + tetradecanoyldihydroxyacetone phosphate
show the reaction diagram
-
i.e. myristoyl-CoA
-
-
?
additional information
?
-
-
the enzyme is involved in the first step of plasmalogen biosynthesis, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
show the reaction diagram
enzyme is involved in biosynthesis of plasmalogens, regulating enzyme
-
-
?
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
show the reaction diagram
additional information
?
-
-
the enzyme is involved in the first step of plasmalogen biosynthesis, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithio-bis(2-nitrobenzoate)
chymotrypsin
-
intact vesicles
-
deoxycholate
glycerol 3-phosphate
Mercuridextran
-
intact microsomes
-
N-ethylmaleimide
Triton X-100
Trypsin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
glycerol 3-phosphate
-
-
additional information
additional information
-
values for enzymes from various tissues
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.861
-
pH 7.4, partially purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
assay at
5.5
-
membrane-bound peroxisomal enzyme
5.7 - 6
-
intact peroxisomes
6.5 - 8
-
peroxisomal enzyme
7
-
purified microsomes
7 - 8
-
mitochondrial enzyme
7.5
-
microsomal enzyme
additional information
-
overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 8.5
-
about half-maximal activity at pH 5.1 and pH 8.5
5.5 - 9.5
-
about half-maximal activity at pH 5.5 and pH 9.5
6.5 - 8.5
-
about half-maximal activity at pH 6.5 and pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male Wistar rats
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in internal structures of cerebellum, hippocampus, and corpus callosum
Manually annotated by BRENDA team
enzyme expression throughout liver tissue
Manually annotated by BRENDA team
-
in situ hybridization of DHAP-AT mRNA is performed on rat eye sections. DHAP-AT is highly expressed in the inner segment of photoreceptors and in the retinal pigment epithelium, suggesting two distinct sites for plasmalogens biosynthesis
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GNPAT_RAT
678
0
77076
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
gel filtration
additional information
-
amino acid sequence determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
immunological, SDS-PAGE and amino acid sequencing analysis of partially purified protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44
-
t1/2: 10 min
50
-
intact microsomes: 25% loss of activity after 30 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing, crude preparation, stable to
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by subcellular fractionation
-
peroxisomal, partial
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
peroxisomal enzyme can be used as marker enzyme for peroxisomal membrane due to insensitivity to glycerol-3-phosphate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ballas, L.M.; Bell, R.M.
Topography of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles
Biochim. Biophys. Acta
665
586-595
1981
Rattus norvegicus
Manually annotated by BRENDA team
Bell, R.M.; Coleman, R.A.
Enzymes of triacylglycerol formation in mammals
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
16
87-111
1983
Oryctolagus cuniculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Bates, E.J.; Saggerson, E.D.
A study of the glycerol phosphate acyltransferase and dihydroxyacetone phosphate acyltransferase activities in rat liver mitochondrial and microsomal fractions. Relative distribution in parenchymal and non-parenchymal cells, effects of N-ethylmaleimide, palmitoyl-coenzyme A concentration, starvation, adrenalectomy and anti-insulin serum treatment
Biochem. J.
182
751-762
1979
Cavia porcellus, Cavia porcellus Hartley, Rattus norvegicus
Manually annotated by BRENDA team
Datta, N.S.; Hajra, A.K.
Does microsomal glycerophosphate acyltransferase also catalyze the acylation of dihydroxyacetone phosphate?
FEBS Lett.
176
264-268
1984
Rattus norvegicus
Manually annotated by BRENDA team
Bell, R.M.
Enzymes of glycerolipid synthesis in eukaryotes
Annu. Rev. Biochem.
49
459-487
1980
Cavia porcellus, Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Schlossman, D.M.; Bell, R.M.
Microsomal sn-glycerol 3-phosphate and dihydroxyacetone phosphate acyltransferase activities from liver and other tissues
Arch. Biochem. Biophys.
182
737-742
1977
Rattus norvegicus
-
Manually annotated by BRENDA team
Declercq, P.E.; Haagsman, H.P.; Van Veldhoven, P.; Debeer, L.J.; Van Golde, L.M.G.; Mannaerts, G.P.
Rat liver dihydroxyacetone-phosphate acyltransferases and their contribution to glycerolipid synthesis
J. Biol. Chem.
259
9064-9075
1984
Rattus norvegicus
Manually annotated by BRENDA team
Hardeman, D.; Van den Bosch, H.
Rat liver dihydroxyacetone-phosphate acyltransferase: enzyme characteristics and localization studies
Biochim. Biophys. Acta
963
1-9
1988
Rattus norvegicus
Manually annotated by BRENDA team
Causeret, C.; Bentejac, M.; Albet, S.; Teubner, B.; Bugaut, M.
Copurification of dihydroxyacetone-phosphate acyl-transferase and other peroxisomal proteins from liver of fenofibrate-treated rats
Biochimie
79
423-433
1997
Rattus norvegicus
Manually annotated by BRENDA team
Singh, H.; Beckman, K.; Poulos, A.
Exclusive localization in peroxisomes of dihydroxyacetone phosphate acyltransferase and alkyl-dihydroxyacetone phosphate synthase in rat liver
J. Lipid Res.
34
467-477
1993
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Andre, A.; Tessier, C.; Bretillon, L.; Sebedio, J.L.; Chardigny, J.M.
In situ hybridization of dihydroxyacetone phosphate acyltransferase, the regulating enzyme involved in plasmalogen biosynthesis
Brain Res. Mol. Brain Res.
136
142-147
2005
Rattus norvegicus (Q9ES71)
Manually annotated by BRENDA team
Andre, A.; Juaneda, P.; Sebedio, J.L.; Chardigny, J.M.
Plasmalogen metabolism-related enzymes in rat brain during aging: influence of n-3 fatty acid intake
Biochimie
88
103-111
2006
Rattus norvegicus
Manually annotated by BRENDA team
Acar, N.; Gregoire, S.; Andre, A.; Juaneda, P.; Joffre, C.; Bron, A.M.; Creuzot-Garcher, C.P.; Bretillon, L.
Plasmalogens in the retina: In situ hybridization of dihydroxyacetone phosphate acyltransferase (DHAP-AT) - the first enzyme involved in their biosynthesis - and comparative study of retinal and retinal pigment epithelial lipid composition
Exp. Eye Res.
84
143-151
2007
Rattus norvegicus
Manually annotated by BRENDA team