Any feedback?
Information on EC 2.3.1.15 - glycerol-3-phosphate 1-O-acyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P97564
for references in articles please use BRENDA:EC2.3.1.15Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.15 glycerol-3-phosphate 1-O-acyltransferaseIUBMB Comments
Acyl-[acyl-carrier protein] can also act as acyl donor. The enzyme acts only on derivatives of fatty acids of chain length larger than C10.
Specify your search results
Word Map
- 2.3.1.15
-
gpats
- triacylglycerols
- phospholipid
-
phosphatidic
- glycerolipids
- acyl-coas
- triglyceride
- diacylglycerol
- adipose
-
lysophosphatidic
- peroxisome
-
lipogenesis
-
lipogenic
- adipocytes
- palmitate
- sterol
- phosphatidylcholine
- palmitoyl-coa
-
phosphohydrolase
- glycerophospholipids
- carnitine
- steatosis
- esterification
- stearoyl-coa
- dihydroxyacetone
-
1-acylglycerol-3-phosphate
- cutin
- srebp-1
- phosphatidylglycerol
- palmitoyltransferase
- oleoyl-coa
-
acyl-acyl
- cytidylyltransferase
- squash
-
desaturase-1
- monoacylglycerol
- protein-1c
- acaca
- suberin
- synthesis
- nutrition
-
cholinephosphotransferase
-
insig1
-
lipins
- medicine
- energy production
- biotechnology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glycerol-3-phosphate acyltransferase, gpat1, glycerophosphate acyltransferase, sn-glycerol-3-phosphate acyltransferase, gpat2, gpat3, gpat4, agpat6, agpat, gat1p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycerol-3-phosphate acyltransferase 1
four isoenzymes are identified in mammals
3-glycerophosphate acyltransferase
-
-
-
-
ACP:sn-glycerol-3-phosphate acyltransferase
-
-
-
-
acyltransferase, glycerol phosphate
-
-
-
-
alpha-glycerophosphate acyltransferase
-
-
-
-
glycerol 3-phosphate acyltransferase
-
-
-
-
glycerol phosphate acyltransferase
-
-
-
-
glycerol phosphate transacylase
-
-
-
-
glycerol-3-phosphate acyltransferase 2
-
four isoenzymes are identified in mammals
glycerophosphate acyltransferase
glycerophosphate transacylase
-
-
-
-
GPAT2
Sn-glycerol 3-phosphate acyltransferase
-
-
-
-
glycerophosphate acyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase
Acyl-[acyl-carrier protein] can also act as acyl donor. The enzyme acts only on derivatives of fatty acids of chain length larger than C10.
CAS REGISTRY NUMBER
COMMENTARY
9029-96-3
-
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
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
docosahexaenoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-docosahexaenoyl-sn-glycerol 3-phosphate
-
-
-
?
eicosapentaenoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-eicosapentaenoyl-sn-glycerol 3-phosphate
-
-
-
?
fatty acyl-CoA + glycerol-3-phosphate
CoA + lysophosphatidic acid
-
-
-
-
?
n-decanoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-n-decanoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + glycerol 3-phosphate
CoA + 1-palmitoyl-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
exclusively acylates glycerol 3-phosphate at the C-1-position
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
no acyl-donors are hexanoyl-CoA, octanoyl-CoA
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
saturated acyl-CoAs preferred
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
saturated acyl-CoAs preferred
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
initial reaction of phosphoglycerol biosynthesis
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
the enzyme catalyzes the first and committed step in the synthesis of glycerophospholipids and TAG from sn-glycerol-3-phosphate
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
the enzyme catalyzes the first and committed step in the synthesis of glycerophospholipids and triacylglycerol from sn-glycerol-3-phosphate
-
-
?
arachidonoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
arachidonoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
arachidonoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
linoleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
linoleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-linoleoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
linoleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-linoleoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
linoleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-linoleoyl-sn-glycerol 3-phosphate
-
2% of activity with palmitoyl-CoA
-
-
?
myristoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-myristoyl-sn-glycerol 3-phosphate
-
-
-
-
?
myristoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-myristoyl-sn-glycerol 3-phosphate
-
i.e. tetradecanoyl-CoA
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
high activity
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
7% of activity with palmitoyl-CoA
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
i.e. lysophosphatidic acid
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
i.e. n-hexadecanoyl-CoA, best substrate
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
i.e. n-hexadecanoyl-CoA, best substrate
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
best acyl donor
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
best acyl donor
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
mitochondrial enzyme, preferred over oleoyl-CoA
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
palmitoyl-CoA is preferred over oleoyl-CoA only in presence of albumin or acyl-CoA binding protein ACBP in young rat livers
-
-
?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
-
-
-
?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
-
-
-
?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
-
-
-
-
?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
-
poor substrate
-
?
additional information
?
-
-
in biochemical studies, saturated fatty acyl-CoAs are preferred approximately 2fold over unsaturated fatty acyl-CoAs as GPAT1 substrates. Esterification occurs at the sn-1 position of glycerol 3-phosphate
-
-
?
additional information
?
-
in biochemical studies, saturated fatty acyl-CoAs are preferred approximately 2fold over unsaturated fatty acyl-CoAs as GPAT1 substrates. Esterification occurs at the sn-1 position of glycerol 3-phosphate
-
-
?
additional information
?
-
-
aging and acyl-CoA binding protein alter mitochondrial enzyme activity
-
-
?
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 + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
high activity
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
-
?
additional information
?
-
-
aging and acyl-CoA binding protein alter mitochondrial enzyme activity
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
initial reaction of phosphoglycerol biosynthesis
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
the enzyme catalyzes the first and committed step in the synthesis of glycerophospholipids and TAG from sn-glycerol-3-phosphate
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
the enzyme catalyzes the first and committed step in the synthesis of glycerophospholipids and triacylglycerol from sn-glycerol-3-phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phenylglyoxal
1 mM, 88% and 59% inhibition of microsomal and mitochondrial acyltransferase, respectively
2,3-Butanedione
5 mM, 54% and 21% inhibition of microsomal and mitochondrial acyltransferase respectively
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonic acid
-
trivial name CHAPS, complete inhibition
aminophenylboronate
mixed-type inhibition of microsomal and mitochondrial acyltransferase vs. glycerol 3-phosphate
diethyldicarbonate
0.3 mM, approx. 67% inhibition of microsomal acyltransferase, approx. 40% inhibition of mitochondrial acyltransferase, approx. 60% inhibition of recombinant mitochondrial acyltransferase, activity is restored to approx 50% by hydroxylamine
Phenylglyoxal
1 mM, 88% and 59% inhibition of microsomal and mitochondrial acyltransferase, respectively
Trypsin
-
0.04 mg/ml, approx. 80% inhibition of microsomal enzyme within 3 min at 37°C, inhibition of the mitochondrial enzyme only in the presence of 0.05% deoxycholate or 0.1% Triton X-100
-
5,5'-dithiobis(2-nitro-benzoate)
-
inhibition of microsomal enzyme, mitochondrial enzyme is not inhibited
diacylglycerophosphate
-
i.e. phosphatidic acid, inhibition of mitochondrial enzyme
iodoacetamide
-
strong inhibition of microsomal enzyme, mitochondrial enzyme is not inhibited
Monoacylglycerophosphate
-
i.e. lysophosphatidic acid, inhibition of mitochondrial enzyme
N-ethylmaleimide
-
0.5-10 mM, 80-90% inhibition of microsomal acyltransferase, mitochondrial acyltransferase is not inhibited
N-ethylmaleimide
-
strong inhibition of microsomal isozyme, mitochondrial enzyme is not inhibited
N-ethylmaleimide
-
4 mM, approx. 50% inhibition of the solubilized acyltransferase, membrane-bound enzyme is not inhibited
Polymyxin B
-
0.5 mg/ml, approx. 75% inhibition of microsomal enzyme, slight stimulation of mitochondrial enzyme
additional information
-
microsomal isozyme, not inhibited by sn-1,2-diolein, 1,2-dioleoylglycerol ether, dioleoylphosphatidic acid
-
additional information
-
mitochondrial enzyme, not inhibited by N-ethylmaleimide
-
additional information
-
liver microsomal enzyme is inhibited by all proteases
-
additional information
-
liver mitochondrial enzyme, not inhibited by trypsin and chymotrypsin
-
additional information
-
mitochondrial enzyme, not inhibited by bromelain, papain, pronase and trypsin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetone
-
activation of mitochondrial enzyme, inhibition of microsomal enzyme
asolectin
-
i.e. crude mixture of soybean phospholipids, activation of mitochondrial enzyme
-
Non-site-specific proteases
-
activation, e.g. proteinase K, subtilisin, not chymotrypsin, trypsin, mitochondrial enzyme, degree of inhibition increases with decreasing ionic strength
-
phosphatidylglycerol
-
highest activation of reconstituted mitochondrial acyltransferase in the presence of Lubrol PX
spermidine
-
activates about 3.5fold in presence of 0.1 mg/ml bovine serum albumin
spermine
-
activates about 3fold in presence of 0.1 mg/ml bovine serum albumin
phosphatidylcholine
-
i.e. lecithin, activation of mitochondrial enzyme
phosphatidylethanolamine
-
activation of reconstituted mitochondrial acyl transferase
Polymyxin B
-
activation of mitochondrial enzyme, inhibition of microsomal enzyme
Polymyxin B
-
antibiotic, reversible binding, stimulation via enhanced extraction of lysophosphatidic acid, maximal at 60%, the acyl side group does not play a role in stimulation, addition of bovine serum albumin is highly required for stimulation, in absence of bovine serum albumin the antibiotic is slightly inhibitory, addition of Mg2+ enhances the stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.46
glycerol 3-phosphate
-
mitochondrial acyl transferase reconstituted in 1,2-dioleoylphosphatidylglycerol
0.82
glycerol 3-phosphate
-
mitochondrial acyl transferase reconstituted in asolectin
0.93
glycerol 3-phosphate
-
mitochondrial acyl transferase reconstituted in 1,2-dipalmitoylphosphatidylglycerol
3.9
glycerol 3-phosphate
-
fixed substrate concentration: 0.08 mM palmitoyl-CoA, without addition of insulin, Vmax: 6.1 nmol/min/mg
7.2
glycerol 3-phosphate
-
fixed substrate concentration: 0.02 mM palmitoyl-CoA, with addition of insulin, Vmax: 7.2 nmol/min/mg
16.4
glycerol 3-phosphate
-
fixed substrate concentration: 0.08 mM palmitoyl-CoA, with addition of insulin, Vmax: 16.6 nmol/min/mg
0.012
myristoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dioleoylphosphatidylglycerol
0.016
myristoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dipalmitoylphosphatidylglycerol
0.016
myristoyl-CoA
-
mitochondrial acyl transferase reconstituted in asolectin
0.0084
oleoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dioleoylphosphatidylglycerol
0.013
oleoyl-CoA
-
mitochondrial acyl transferase reconstituted in asolectin
0.015
oleoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dipalmitoylphosphatidylglycerol
0.0031
palmitoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dioleoylphosphatidylglycerol
0.006
palmitoyl-CoA
-
mitochondrial acyl transferase reconstituted in asolectin
0.007
palmitoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dipalmitoylphosphatidylglycerol
0.007
palmitoyl-CoA
-
value below 0.007 mM, fixed substrate concentration: 0.002 mM glycerol-3-phosphate, without addition of insulin, Vmax: 2.4 nmol/min/mg
0.0264
palmitoyl-CoA
-
fixed substrate concentration: 0.002 mM glycerol-3-phosphate, with addition of insulin, Vmax: 14.1 nmol/min/mg
0.0064
stearoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dioleoylphosphatidylglycerol
0.011
stearoyl-CoA
-
mitochondrial acyl transferase reconstituted in asolectin
0.013
stearoyl-CoA
-
mitochondrial acyl transferase reconstituted in 1,2-dipalmitoylphosphatidylglycerol
additional information
additional information
-
insulin treatment of rat primary adipocytes acutely increases the Km and Vmax of GPAT1 for its substrates, which may be mediated through protein phosphorylation
-
additional information
additional information
insulin treatment of rat primary adipocytes acutely increases the Km and Vmax of GPAT1 for its substrates, which may be mediated through protein phosphorylation
-
additional information
additional information
-
solubilization increases Km of mitochondrial acyltransferase for glycerol 3-phosphate
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00016
-
contact sites obtained from mitochondria, subfraction of crude mitochondria
0.0003
-
activity in rat liver membranes after inhibiting endoplasmic reticulum GPAT with N-ethylmaleimide, rats are treated with Ad-EGFP
0.00065
0.00083
-
activity in rat liver membranes after inhibiting endoplasmic reticulum GPAT with N-ethylmaleimide, rats are treated with Ad-GPAT1
0.0029
-
contact sites obtained from mitochondria, subfraction of pure mitochondria
0.19
-
mitochondrial acyltransferase reconstituted in phosphatidylglycerol/phosphatidylethanolamine mixture
additional information
additional information
-
activity in young and old livers in absence or presence of bovine serum albumin or acyl-CoA binding protein, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 9
-
both microsomal and mitochondrial enzymes exhibit a broad optimum
7.4
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
epididymal fat, increased activity upon cessation of wheel running. Increase in mtGPAT protein might contribute to the overshoot in triacylglycerol synthesis
epididymal fat, increased activity upon cessation of wheel running. Increase in mtGPAT protein might contribute to the overshoot in triacylglycerol synthesis
expression only in primary spermatocytes. During rat sexual maturation, both the testicular TAG content and the arachidonic acid content in the triacylglycerol fraction peak at 30 days, matching the highest expression of Gpat2 mRNA and protein
aging reduces glycerol-3-phosphate acyltransferase activity in activated rat splenic T-lymphocytes
-
-
-
hepatic overexpression of glycerol-sn-3-phosphate acyltransferase 1 in rats causes insulin resistance
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
significant acyltransferase activity in inner membrane
-
-
-
-
mtGPAT1 has two transmembrane domains (TMDs) (aa 472493 and aa 576592) with both the N- and C-termini facing the cytosol and a loop (aa 494575) facing the intermembrane space
-
N- and C-termini and the active site of acyltransferase face the cytosolic face of the outer mitochondrial membrane, proposed model for orientation
-
spans transverse plane of outer membrane
-
activity with palmitoyl-CoA is reduced in mitochondria of aged livers
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
upon stable overexpression of isoform Gpat1, lysophosphatidic acid levels in CHO-GPAT1 cells are 6fold higher than in wild-type CHO cells, and the mRNA abundance of CD36, a target of peroxisome proliferator activated receptor PPARgamma, is 2fold higher. PPARgamma activity is higher in the cells that overexpress isoform GPAT1. PPARgamma activity is further enhanced in CHO-GPAT1 cells treated with the PPARgamma ligand troglitazone. Extracellular LPA, phosphatidic acid or a membrane-permeable diacylglycerol have no effect
physiological function
malfunction
GPAT1 overexpression in rat primary hepatocytes results in the increased incorporation of exogenous fatty acids into triacylglycerol and phospholipids and reduced rate of beta-oxidation
malfunction
in GPAT1-overexpressing rats, hepatic acyl-CoA content and plasma beta-hydroxybutyrate concentration are similar to those of control rats
physiological function
in contrast to Gpat1, Gpat2 mRNA does not increase in liver of rats refed a high-sucrose diet after fasting, suggesting less contribution of GPAT2 to diet-induced hepatic TAG synthesis
physiological function
-
treatment of primary rat adipocytes with insulin acutely affects the activity of mtGPAT1 by increasing VMAX and KM for the substrates glycerol-3-phosphate and palmitoyl-CoA
physiological function
isoform GPAT2 overexpression in CHO-K1 cells increased arachidonoyl-CoA esterification and accumulation of triacylglycerols. GPAT2 expression is linked to arachidonoyl-CoA incorporation into triacylglycerols in spermatogenic germ cells
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). GPAT1_RAT
828
0
93715
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
proteolytic cleavage of isolated mitochondrial membranes and mass spectrometric peptide sequencing identify in vivo phosphorylation of serine 632 and serine 639 in mtGPAT1. These phosphorylation sites correspond to casein kinase-2 consensus sequences
side-chain modification
-
activity of microsomal enzyme is probably regulated by phosphorylation-dephosphorylation
phosphoprotein
direct phosphorylation of mrGPAT1 in yound T-lymphocytes
phosphoprotein
phosphorylation may be involved in increased mitochondrial GPAT activity in stimulated T-lymphocytes
phosphoprotein
insulin treatment of rat primary adipocytes acutely increases the Km and Vmax of GPAT1 for its substrates, which may be mediated through protein phosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
truncation of the C-terminal domain and characterization of the properties of the resulting mutants expressed in CHO cells. Although the mutants are overexpressed, none of them confers GPAT activity. The loss of activity is not due to the miss-targeting of the proteins. The C-terminal domain is necessary for mtGPAT1 activity, and probably contributes to catalysis or substrate binding
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mitochondria are isolated from rat liver by differential centrifugation
mitochondria and submitochondrial fractions are purified by gradient centrifugation, radiolabeled GPAT1 is synthesized by an in vitro transcription-translation system
-
mitochondrial enzyme, Sepharose Q, BioGel HAT, octyl-Sepharose CL-4B, partial purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the promotor regions, distal and proximal, are cloned into the promotorless mammalian expression vector pGL3-basic that contains firefly luciferase as the reporter gene
overexpression of FLAG-tagged mitochondrial isozymes in HEK293 cells and in primary hepatocytes from fasted rats via adenovirus transfection system, leading to increased enzyme activity and incorporation of added oleate into triacylglycerol, the triacylgycerol is secreted from the recombinant hepatocytes if higher concentrated, phospholipid composition in hepatocytes, overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution in asolection or phosphatidylglycerol/phosphatidylethanolamine mixture
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
it has been implicated as one of the enzymes that can play a role in obesity and diabetes
medicine
-
major finding of the study is that overexpressing GPAT in liver causes hepatic steatosis and hepatic insulin resistance in the absence of obesity or high-fat feeding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bramley, P.M.; Grigor, M.R.
Acyl-CoA:sn-glycerol 3-phosphate acetyltransfrase isozymes in rat mammary gland
Biochem. Int.
5
199-204
1982
Rattus norvegicus
-
Bell, R.M.; Coleman, R.A.
Enzymes of triacylglycerol formation in mammals
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
16
87-111
1983
Escherichia coli, Rattus norvegicus
-
Haldar, D.; Vancura, A.
Glycerophosphate acyltransferase from liver
Methods Enzymol.
209
64-72
1992
Rattus norvegicus
Yamashita, S.; Numa, S.
Partial purification and properties of glycerophosphate acyltransferase from rat liver. Formation of 1-acylglycerol 3-phosphate from sn-glycerol 3-phosphate and palmityl coenzyme A
Eur. J. Biochem.
31
565-573
1972
Rattus norvegicus, Rattus norvegicus Wistar
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
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Monroy, G.; Chroboczek Kelker, H.; Pullman, M.E.
Partial purification and properties of an acyl coenzyme A:sn-glycerol 3-phosphate acyltransferase from rat liver mitochondria
J. Biol. Chem.
248
2845-2852
1973
Rattus norvegicus
Carroll, M.A.; Morris, P.E.; Grosjean, C.D.; Anzalone, T.; Haldar, D.
Further distinguishing properties of mitochondrial and microsomal glycerophosphate acyltransferase and the transmembrane location of the mitochondrial enzyme
Arch. Biochem. Biophys.
214
17-25
1982
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Coleman, R.A.
Hepatic sn-glycerol-3-phosphate acyltransferases: effect of monoacylglycerol analogs on mitochondrial and microsomal activities
Biochim. Biophys. Acta
963
367-374
1988
Rattus norvegicus
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, Rattus norvegicus Sprague-Dawley
Yamashita, S.; Numa, S.
Glycerophosphate acyltransferase from rat liver
Methods Enzymol.
71
550-554
1981
Rattus norvegicus, Rattus norvegicus Wistar
Mitchell, J.R.D.; Saggerson, E.D.
A study of glycerolphosphate acyltransferase in rat liver mitochondria - submitochondrial localization and some properties of the solubilized enzyme
Int. J. Biochem.
26
181-187
1994
Rattus norvegicus
Vancura, A.; Haldar, D.
Purification and characterization of glycerophosphate acyltransferase from rat liver mitochondria
J. Biol. Chem.
269
27209-27215
1994
Rattus norvegicus
Dircks, L.K.; Sul, H.S.
Mammalian mitochondrial glycerol-3-phosphate acyltransferase
Biochim. Biophys. Acta
1348
17-26
1997
Cavia porcellus, Mus musculus, Rattus norvegicus
Ganesh Bhat, B.; Wang, P.; Kim, J.H.; Black, T.M.; Lewin, T.M.; Fiedorek, F.T., Jr.; Coleman, R.A.
Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and characterization of the cDNA and expressed protein
Biochim. Biophys. Acta
1439
415-423
1999
Escherichia coli, Rattus norvegicus, Rattus norvegicus (P97564)
Gonzalez-Baro, M.R.; Granger, D.A.; Coleman, R.A.
Mitochondrial glycerol phosphate acyltransferase contains two transmembrane domains with the active site in the N-terminal domain facing the cytosol
J. Biol. Chem.
276
43182-43188
2001
Rattus norvegicus
Lewin, T.M.; Wang, S.; Nagle, C.A.; Van Horn, C.G.; Coleman, R.A.
Mitochondrial glycerol-3-phosphate acyltransferase-1 directs the metabolic fate of exogenous fatty acids in hepatocytes
Am. J. Physiol.
288
E835-844
2005
Rattus norvegicus
Kannan, L.; Knudsen, J.; Jolly, C.A.
Aging and acyl-CoA binding protein alter mitochondrial glycerol-3-phosphate acyltransferase activity
Biochim. Biophys. Acta
1631
12-16
2003
Rattus norvegicus
Roy, A.; Guha, N.; Veras, I.D.; Chakraborty, S.; Haldar, D.
Stimulation of rat liver mitochondrial sn-glycerol-3-phosphate acyltransferase by polymyxin B via enhanced extraction of lysophosphatidic acid
Lipids
38
965-972
2003
Rattus norvegicus
Kump, D.S.; Laye, M.J.; Booth, F.W.
Increased mitochondrial glycerol-3-phosphate acyltransferase protein and enzyme activity in rat epididymal fat upon cessation of wheel running
Am. J. Physiol. Endocrinol. Metab.
290
E480-E489
2006
Rattus norvegicus (P97564)
Pellon-Maison, M.; Coleman, R.A.; Gonzalez-Baro, M.R.
The C-terminal region of mitochondrial glycerol-3-phosphate acyltransferase-1 interacts with the active site region and is required for activity
Arch. Biochem. Biophys.
450
157-166
2006
Rattus norvegicus
Collison, L.M.; Kannan, L.; Onorato, T.M.; Knudsen, J.; Haldar, D.; Jolly, C.A.
Aging reduces glycerol-3-phosphate acyltransferase activity in activated rat splenic T-lymphocytes
Biochim. Biophys. Acta
1687
164-172
2005
Rattus norvegicus (P97564)
Collison, L.W.; Jolly, C.A.
Phosphorylation regulates mitochondrial glycerol-3-phosphate-1 acyltransferase activity in T-lymphocytes
Biochim. Biophys. Acta
1761
129-139
2006
Rattus norvegicus (P97564)
Nagle, C.A.; An, J.; Shiota, M.; Torres, T.P.; Cline, G.W.; Liu, Z.X.; Wang, S.; Catlin, R.L.; Shulman, G.I.; Newgard, C.B.; Coleman, R.A.
Hepatic overexpression of glycerol-sn-3-phosphate acyltransferase 1 in rats causes insulin resistance
J. Biol. Chem.
282
14807-14815
2007
Rattus norvegicus
Aneja, K.K.; Guha, P.; Shilpi, R.Y.; Chakraborty, S.; Schramm, L.M.; Haldar, D.
The presence of distal and proximal promoters for rat mitochondrial glycerol-3-phosphate acyltransferase
Arch. Biochem. Biophys.
470
35-43
2008
Rattus norvegicus (P97564)
Pellon-Maison, M.; Montanaro, M.A.; Coleman, R.A.; Gonzalez-Baro, M.R.
Mitochondrial glycerol-3-P acyltransferase 1 is most active in outer mitochondrial membrane but not in mitochondrial associated vesicles (MAV)
Biochim. Biophys. Acta
1771
830-838
2007
Rattus norvegicus
Takeuchi, K.; Reue, K.
Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis
Am. J. Physiol. Endocrinol. Metab.
296
E1195-E1209
2009
Rattus norvegicus, Rattus norvegicus (P97564), Mus musculus (Q14DK4), Mus musculus (Q61586), Mus musculus (Q8C0N2), Mus musculus (Q8K2C8), Mus musculus, Homo sapiens (Q53EU6), Homo sapiens (Q86UL3), Homo sapiens
Bronnikov, G.E.; Aboulaich, N.; Vener, A.V.; Stralfors, P.
Acute effects of insulin on the activity of mitochondrial GPAT1 in primary adipocytes
Biochem. Biophys. Res. Commun.
367
201-207
2008
Rattus norvegicus
Stapleton, C.; Mashek, D.; Wang, S.; Nagle, C.; Cline, G.; Thuillier, P.; Leesnitzer, L.; Li, L.; Stimmel, J.; Shulman, G.; Coleman, R.
Lysophosphatidic acid activates peroxisome proliferator activated receptor-gamma in CHO cells that over-express glycerol 3-phosphate acyltransferase-1
PLoS ONE
6
e18932
2011
Rattus norvegicus (P97564)
Cattaneo, E.R.; Pellon-Maison, M.; Rabassa, M.E.; Lacunza, E.; Coleman, R.A.; Gonzalez-Baro, M.R.
Glycerol-3-phosphate acyltransferase-2 is expressed in spermatic germ cells and incorporates arachidonic acid into triacylglycerols
PLoS ONE
7
e42986
2012
Rattus norvegicus (D3ZI76)
EXTERNAL LINKS (specific for EC-Number 2.3.1.15)
Transporter Classification Database (TCDB): 9.B.31.1.1
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
