Information on EC 2.3.1.42 - glycerone-phosphate O-acyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.42
-
RECOMMENDED NAME
GeneOntology No.
glycerone-phosphate O-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
show the reaction diagram
; A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA
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-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycerophospholipid metabolism
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-
phosphatidate biosynthesis (yeast)
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plasmalogen biosynthesis
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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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
V1
-
-
Manually annotated by BRENDA team
no activity in Schizosaccharomyces pombe
-
-
-
Manually annotated by BRENDA team
gene TTHERM_00221020
UniProt
Manually annotated by BRENDA team
gene TTHERM_00221020
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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 + dihydroxyacetone phosphate
CoA + acyldihydroxyacetone phosphate
show the reaction diagram
acyl-CoA + glycerone phosphate
CoA + 1-acylglycerone phosphate
show the reaction diagram
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
show the reaction diagram
arachidonoyl-CoA + dihydroxyacetone phosphate
CoA + arachidonoyldihydroxyacetone phosphate
show the reaction diagram
cis-9-hexadecenoyl-CoA + dihydroxyacetone phosphate
CoA + cis-9-hexadecenoyldihydroxyacetone phosphate
show the reaction diagram
dihydroxyacetone phosphate + acyl-CoA
1-acyl-glycerone phosphate + CoA
show the reaction diagram
dihydroxyacetone phosphate + arachidoyl-CoA
1-arachidoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + lauroyl-CoA
1-lauroyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + linoleoyl-CoA
1-linoleoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + myristoyl-CoA
1-myristoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + oleoyl-CoA
1-oleoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + palmitoleoyl-CoA
1-palmitoleoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + palmitoyl-CoA
palmitoyl-glycerone phosphate + CoA
show the reaction diagram
dihydroxyacetone phosphate + stearoyl-CoA
1-stearoyl-glycerone phosphate + CoA
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + dihydroxyacetone phosphate
CoA + dodecanoyldihydroxyacetone phosphate
show the reaction diagram
elaidoyl-CoA + dihydroxyacetone phosphate
CoA + elaidoyldihydroxyacetone phosphate
show the reaction diagram
-
poor substrate, mitochondrial enzyme
-
-
?
heptadecanoyl-CoA + dihydroxyacetone phosphate
CoA + heptadecanoyldihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
lignoceroyl-CoA + dihydroxyacetone phosphate
CoA + lignoceroyldihydroxyacetone phosphate
show the reaction diagram
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poor substrate
-
-
?
linoleoyl-CoA + dihydroxyacetone phosphate
CoA + linoleoyldihydroxyacetone phosphate
show the reaction diagram
nonadecanoyl-CoA + dihydroxyacetone phosphate
CoA + nonadecanoyldihydroxyacetone phosphate
show the reaction diagram
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poor substrate
-
-
?
nonanoyl-CoA + dihydroxyacetone phosphate
CoA + nonanoyldihydroxyacetone phosphate
show the reaction diagram
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poor substrate
-
-
?
octadecenoyl-CoA + dihydroxyacetone phosphate
CoA + heptadecenoyldihydroxyacetone phosphate
show the reaction diagram
-
-
-
?
oleoyl-CoA + dihydroxyacetone phosphate
CoA + oleoyldihydroxyacetone phosphate
show the reaction diagram
oleoyl-CoA + glycerone phosphate
CoA + 1-oleoyl-glycerone phosphate
show the reaction diagram
palmitoleyl-CoA + glycerone phosphate
CoA + 1-palmitoleyl-glycerone phosphate
show the reaction diagram
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
show the reaction diagram
palmitoyl-CoA + glycerone phosphate
CoA + 1-palmitoyl-glycerone phosphate
show the reaction diagram
pentadecanoyl-CoA + dihydroxyacetone phosphate
CoA + pentadecanoyldihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + dihydroxyacetone phosphate
CoA + stearoyldihydroxyacetone phosphate
show the reaction diagram
stearoyl-CoA + glycerone phosphate
CoA + 1-stearoyl-glycerone phosphate
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + dihydroxyacetone phosphate
CoA + tetradecanoyldihydroxyacetone phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + 1-acylglycerone phosphate
show the reaction diagram
acyl-CoA + glycerone phosphate
CoA + acylglycerone phosphate
show the reaction diagram
dihydroxyacetone phosphate + acyl-CoA
1-acyl-glycerone phosphate + CoA
show the reaction diagram
palmitoyl-CoA + dihydroxyacetone phosphate
CoA + monopalmitoyldihydroxyacetone phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithio-bis(2-nitrobenzoate)
acetaldehyde
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above 0.01 M, microsomal enzyme, above 0.2 M, solubilized peroxisomal enzyme
bovine serum albumin
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weak
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Ca2+
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in crude enzyme extract
cholate
Chymotrypsin
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intact vesicles
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coenzyme A
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kinetics
deoxycholate
DL-carnitine
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glycerol 3-phosphate
iodoacetamide
Mercuridextran
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intact microsomes
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Mg2+
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in crude enzyme extract
Mn2+
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in crude enzyme extract
N-ethylmaleimide
p-Chloromercuriphenylsulfonic acid
palmitoyl-CoA
phosphatidic acid
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phosphatidylethanolamine
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above 1.5 mM
phosphatidylinositol
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phosphatidylserine
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above 1.5 mM
Tris-maleate buffer
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pH 5.0-6.0
Triton X-100
Trypsin
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Tween 20
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetaldehyde
asolectin
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activation, i.e. crude soybean phospholipid preparation containing phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol
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bovine serum albumin
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activation, by inhibiting the formation of palmitoyl-CoA micelles
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cholate
deoxycholate
Detergents
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stimulation and solubilization of membrane-bound microsomal activity, e.g. Lubrol WX, cholate and deoxycholate
diphosphate
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30fold activation at 10 mM
Isopropanol
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stimulation
Phospholipid
Triton X-100
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.79
dihydroxyacetone phosphate
0.04 - 0.065
palmitoyl-CoA
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76
CoA
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0.07 - 0.12
glycerol 3-phosphate
additional information
additional information
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values for enzymes from various tissues
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00004 - 0.00008
0.000091
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0.00042
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CHO-K1 wild-type cell
0.00061
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purified enzyme
0.0018
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peroxisomes
0.00245
0.861
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pH 7.4, partially purified enzyme
2.47
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purified enzyme
3.35
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.2
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broad optimum
5.7 - 6
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intact peroxisomes
6.4
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in presence of asolectin
6.5 - 8
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peroxisomal enzyme
7 - 8.2
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broad
7 - 8
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mitochondrial enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 8.5
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about half-maximal activity at pH 5.1 and pH 8.5
5.4 - 7.3
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about half-maximal activity at pH 5.4 and pH 7.3
5.5 - 9
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detectable activity in this range
5.5 - 9.5
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about half-maximal activity at pH 5.5 and pH 9.5
6 - 9
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about half-maximal activity at pH 6.0 and pH 9.0, in the presence of asolectin
6.5 - 8.5
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about half-maximal activity at pH 6.5 and pH 8.5
7.4
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about half-maximal activity above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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CHO-K1 cell line
Manually annotated by BRENDA team
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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000 - 80000
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gel filtration
65000
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1 * 65000, SDS-PAGE
66000
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gel filtration
69000
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x * 69000, SDS-PAGE
72000
-
gel filtration
77190
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DNA sequence determination
90000
-
gel filtration
150000
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fusion protein
210000
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heterooligomeric complex consisting of 3 polypeptides of 76, 72 and 69 kDa, sucrose density gradient centrifugation
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 69000, SDS-PAGE
monomer
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1 * 65000, SDS-PAGE
additional information
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immunological, SDS-PAGE and amino acid sequencing analysis of partially purified protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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significant loss of activity
44
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t1/2: 10 min
50
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intact microsomes: 25% loss of activity after 30 min
51
-
t1/2: 15 min, with asolectin
65
-
inactivation within 15 min, crude peroxisomal preparation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
asolectin stabilizes against inactivation during freezing and thawing
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DEAE-Sephacel chromatography inactivates
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dipalmitoylphosphatidylcholine stabilizes purified enzyme
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freezing inactivates
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freezing, crude preparation, stable to
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heat shock, osmotic shock and freeze-thaw cycles increase enzyme activity at pH 7.5, at pH 5.5 activity is decreased
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heating membranes to 50C prior to assay increases activity of membrane-bound enzyme
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isoelectric focusing inactivates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, up to 1 month
-
2-4C, 30-50% loss of activity after 1 month, DTT stabilizes during storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by subcellular fractionation
-
partial, solubilized with sodium cholate-KCl
-
peroxisomal from placenta, with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, i.e. CHAPS, plus 1 M KCl
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peroxisomal, partial
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with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, i.e. CHAPS, plus 0.15 M NaCl
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with taurocholate
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme cloned from a cDNA library matching EST-clones with peptides from rabbit peroxisomal enzyme, DNA sequence determination
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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
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expression of the human enzyme encoding cDNA in a 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 decreased in both cases
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functional expression in Saccharomyces cerevisiae
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functional expression in Saccharomyces cerevisiae, DNA and amino acid sequence determination
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gene DAT, DNA amd amino acid sequence determination and analysis, DAT functionally complements the lethality resulting from the loss of both dihydroxyacetone phosphate and glycerol-3-phosphate acyltransferase activities in yeast, recombinant DAT exhibits biochemical properties similar to those of the native enzyme of the promastigote stage parasites
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gene TTHERM_00221020, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant transient expression of GFP-tagged truncated bifunctional enzyme in Nicotiana tabacum cv. Petit Havana epidermis, using the Agrobacterium tumefaciens GV3101 strain and used for transient expression system, and transgenic expression in Saccharomyces cerevisiae, the recombinant enzyme's N-terminal FAR-like domain produces both 16:0 and 18:0 fatty alcohols, whereas the C-terminal acyltransferase-like domain is able to rescue the lethal phenotype of the Saccharomyces cerevisiae double mutant cmy228 (gat1DELTAgat2DELTA). Coexpression in Saccharomyces cerevisiae with the alkyl-dihydroxyacetone phosphate synthase from Tetrahymena thermophila results the detection of various glycerolipids with an ether bond. In yeast, GAT1 and GAT2 are the only two acyltransferases acylating the sn-1 position of G3P and DHAP, thus being essential to initiate glycerolipid biosynthesis
genes GAT1 and GAT2, expression in Escherichia coli DH5alpha, Gat1 and Gat2 proteins are glycerol-3-phosphate/dihydroxyacetone phosphate dual substrate-specific sn-1 acyltransferases, amino acid sequence analysis
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PCR-amplification, transfection of Leishmania by electroporation
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K852L
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mutant shows no activity and fails to support normal growth and survival during the stationary phase
additional information
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
medicine
-
DHPAT activity is decreased in fibroblast cell lines from patients with a deficient cytosolic receptor protein PEX5
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