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Information on EC 2.3.1.51 - 1-acylglycerol-3-phosphate O-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q9D517
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2.3.1.51 1-acylglycerol-3-phosphate O-acyltransferaseIUBMB Comments
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
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Word Map
- 2.3.1.51
- adipose
- triacylglycerols
- triglyceride
- lipodystrophy
- phospholipid
- acyl-coas
- lipase
- diacylglycerol
- droplet
- adipocytes
-
berardinelli-seip
-
lipolysis
- glycerolipids
- agpats
- glycerophospholipids
-
chanarin-dorfman
- hypertriglyceridemia
- lysophospholipids
-
seipin
- ichthyosis
-
perilipins
-
acanthosis
-
ichthyosiform
-
nigricans
- erythroderma
-
identification-58
-
kennedy
-
acyl-acyl
-
endophilins
-
lipoatrophy
-
acyl-coa-dependent
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
abhd5, agpat2, lpaat, lysophosphatidic acid acyltransferase, lpaat-beta, agpat1, 1-acylglycerol-3-phosphate o-acyltransferase, agpat3, lpa acyltransferase, agpat4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-acyl-sn-glycero-3-phosphate acyltransferase
-
-
-
-
1-acyl-sn-glycerol 3-phosphate acyltransferase
1-acyl-sn-glycerol-3-phosphate acyltransferase
1-acylglycero-3-phosphate acyltransferase
-
-
-
-
1-acylglycerolphosphate acyltransferase
-
-
-
-
1-acylglycerophosphate acyltransferase
-
-
-
-
acyltransferase, 1-acylglycerol phosphate
-
-
-
-
AGPAT1
AGPAT4
LPAATdelta
lysophosphatidic acid acyltransferase
lysophosphatidic acid-acyltransferase
-
-
-
-
additional information
1-acyl-sn-glycerol 3-phosphate acyltransferase
-
-
-
-
additional information
C4B4E7
the enzyme belongs to the 1-acylglycerol-3-phosphate O-acyltransferase, AGPAT, family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
CAS REGISTRY NUMBER
COMMENTARY
51901-16-7
-
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
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
-
-
-
?
arachidonoyl-CoA + 1-octadecenyl-2-lysophosphatidylinositol
CoA + 1-octadecenyl-2-arachidonoylphosphatidylinositol
C4B4E7
-
-
-
?
arachidonoyl-CoA + 1-oleoyl-2-lysophosphatidylcholine
CoA + 1-oleoyl-2-arachidonoylphosphatidylcholine
C4B4E7
-
-
-
?
arachidonoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
minor substrate
-
-
?
arachidonoyl-CoA + 1-palmitoyl-2-lysophosphatidylinositol
CoA + 1-palmitoyl-2-arachidonoylphosphatidylinositol
C4B4E7
-
-
-
?
arachidonoyl-CoA + 1-stearoyl-2-lysophosphatidic acid
CoA + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
-
-
-
?
docosahexaenoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-docosahexaenoyl-sn-glycerol 3-phosphate
C4B4E7
best substrates
-
-
?
oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
C4B4E7
minor substrate
-
-
?
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-sn-glycerol 3-phosphate
-
-
-
?
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + palmitoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-sn-glycerol 3-phosphate
highest activity
-
-
?
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-CoA + 1-stearoyl-sn-glycerol 3-phosphate
CoA + 1-stearoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + 1-O-alkyl-sn-glycerol 3-phosphate
CoA + ?
-
the activity is approximately half of that toward 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
-
-
-
r
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
arachidonoyl-CoA + 1-arachidonoyl-2-lyso-sn-phosphatidylcholine
CoA + 1,2-diarachidonoyl-sn-phosphatidylcholine
-
-
-
?
arachidonoyl-CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
CoA + 1,2-diarachidonoyl-sn-glycerol 3-phosphate
slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
-
-
?
arachidonoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-arachidonoyl-sn-glycerol 3-phosphate
and oleoyl-CoA, preferred substrates
-
-
?
arachidonoyl-CoA + 1-oleoyl-sn-lysophosphatidylcholine
CoA + 1-oleoyl-2-arachidonoylphosphatidylcholine
-
-
-
?
arachidonoyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-arachidonoyl-sn-glycerol 3-phosphate
slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
-
-
?
arachidonoyl-CoA + 1-palmitoyl-sn-lysophosphatidylcholine
CoA + 1-palmitoyl-2-arachidonoylphosphatidylcholine
-
-
-
?
arachidonoyl-CoA + 1-stearoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-stearoyl-sn-glycerol 3-phosphate
slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
-
-
?
arachidonoyl-CoA + 1-stearoyl-sn-lysophosphatidylcholine
CoA + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphocholine
-
-
-
?
linoleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
linoleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
r
myristoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-myristoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-arachidonoyl-sn-glycerol 3-phosphate
CoA + 1-arachidonoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-arachidonoyl-sn-lysophosphatidylcholine
CoA + 1-arachidonoyl-2-oleoyl-sn-glycero-3-phosphocholine
-
-
-
?
oleoyl-CoA + 1-oleoyl-2-lysophosphatidylcholine
CoA + 1,2-dioleoyl-sn-glycero-3-phosphocholine
-
-
-
?
oleoyl-CoA + 1-palmitoyl-sn-lysophosphatidylcholine
CoA + 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
-
-
-
?
oleoyl-CoA + 1-stearoyl-sn-lysophosphatidylcholine
CoA + 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine
-
-
-
?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
stearoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-stearoyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
preferred donor substrate is arachidonoyl-CoA, no activity with oleoyl-CoA, strong activity with arachidonoyl-CoA and palmitoyl-lysophosphatidic acid, stearoyl-lysophosphatidic acid, oleoyl-lysophosphatidic acid, and octadecenyl-lysophosphatidic acid as acceptors
-
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
-
-
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
AGPAT1 shows strict acyl acceptor specificity for lysophosphatidic acid, acyl-CoA specificity, overview
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
recombinant enzyme can catalyse ATP-independent acyl-CoA synthetic activity and CoA-dependent transacylation activity. Acyl-CoA synthetase is not involved in the process
-
r
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
i.e. lysophosphatidic acid
i.e. phosphatidic acid
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
the expression of AGPATs is linked to skin barrier requirements
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme catalyzes the transfer of the fatty acid from an acyl donor to the sn-2-position of lysophosphatidic acid
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
i.e. lysophosphatidic acid, the recombinant CGI-58 shows preference for arachidonoyl-CoA and oleoyl-CoA, and slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
i.e. phosphatidic acid
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
the enzyme has high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA
-
-
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
and arachidonoyl-CoA, preferred substrates. Slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid
-
-
?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
additional information
?
-
C4B4E7
mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
-
-
?
additional information
?
-
-
mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
-
-
?
additional information
?
-
C4B4E7
isoform LPAAT3 shows a clear preference for 18:1-lyso-PA as acyl acceptor and 22:6-CoA as acyl donor compared to other substrate combinations tested. The respective product sn-1-18:1-sn-2-22:6-phosphatidic acid is almost exclusively formed by LPAAT3. The enzyme shows Michaelis-Menten rate behavior toward 22:6-CoA in the presence of sn-1-18:1-lyso-phosphatidic acid
-
-
?
additional information
?
-
-
isoform LPAAT3 shows a clear preference for 18:1-lyso-PA as acyl acceptor and 22:6-CoA as acyl donor compared to other substrate combinations tested. The respective product sn-1-18:1-sn-2-22:6-phosphatidic acid is almost exclusively formed by LPAAT3. The enzyme shows Michaelis-Menten rate behavior toward 22:6-CoA in the presence of sn-1-18:1-lyso-phosphatidic acid
-
-
?
additional information
?
-
-
the enzyme utilizes both saturated and unsaturated acyl-CoA as an acyl-donor but does not catalyse the transfer of acyl moiety to lysophosphatidylcholine or lyso-platelet-activating factor
-
-
?
additional information
?
-
-
lysophospholipids such as 1-acyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoethanolamine, 1-acyl-sn-glycero-3-phosphoinositol and lysoplatelet-activating factor do not serve as acyl acceptor substrates. Free fatty acids do not serve as acyl donors. The enzyme shows a broad specificity for acyl-CoAs
-
-
?
additional information
?
-
-
reverse reaction of the enzyme: desulfo-CoA and dephospho-COA do not serve as substrates for acyl-CoA synthesis
-
-
?
additional information
?
-
-
CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
-
-
?
additional information
?
-
CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
-
-
?
additional information
?
-
-
the recombinant CoA-dependent His-tagged CGI-58 is active with lysophosphatidic acid, but not with other lysophospholipid or neutral glycerolipid acceptors
-
-
?
additional information
?
-
the recombinant CoA-dependent His-tagged CGI-58 is active with lysophosphatidic acid, but not with other lysophospholipid or neutral glycerolipid acceptors
-
-
?
additional information
?
-
the enzyme interacts specifically with the phospholipid transfer protein StarD10 in vivo and in vitro as well as with one isoform of StarD7 but shows no interaction with StarD2/PC transfer protein
-
-
?
additional information
?
-
in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
-
-
-
additional information
?
-
in vitro, the LPAAT activity of AGPAT1 has a broad specificity for acyl-CoAs, but also has ATP-independent acyl-CoA biosynthetic activity and CoA-dependent transacylation activity. Substrate specificity, overview
-
-
-
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 + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
C4B4E7
-
-
-
?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
C4B4E7
-
-
-
?
acyl-CoA + 1-acyl-lysophosphatidic acid
CoA + 1,2-diacyl-lysophosphatidic acid
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
i.e. lysophosphatidic acid
i.e. phosphatidic acid
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
the expression of AGPATs is linked to skin barrier requirements
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
the enzyme has high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA
-
-
?
additional information
?
-
C4B4E7
mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
-
-
?
additional information
?
-
-
mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor, overview
-
-
?
additional information
?
-
-
CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
-
-
?
additional information
?
-
CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
isozyme AGPAT2 and AGPAT5 expression increase in parallel with both an increase in enzyme activity and permeability barrier formation late in rat epidermal development, acute permeability barrier disruption, by tape-stripping, leads to rapidly increased expression of isozymes AGPAT 1, 2, and 3, reversible by occlusion
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
C4B4E7
high expression level, expression of the enzyme in the testis increases significantly in an age-dependent manner
-
whole, analysis of enzyme mRNA expression, only the transcript of approximately 2 kb length is present. In 7-day embryos both bands of 1.3 and 2 kb are present
-
isozyme AGPAT2 and AGPAT5 expression increase in parallel with both an increase in enzyme activity and permeability barrier formation late in rat epidermal development, acute permeability barrier disruption leads to rapidly increased expression of isozymes AGPAT 1, 2, and 3
-
mAGPAT1, mAGPAT2, mAGPAT3, mAGPAT4 is expressed at low levels, mAGPAT5 expressed at intermediate levels
additional information
-
analysis of enzyme mRNA expression, transcript of approximately 2 kb length dominant
-
mAGPAT1, mAGPAT2, mAGPAT3, mAGPAT2 is undetectable, mAGPAT4 is expressed at high levels, mAGPAT5 expressed at high levels
-
analysis of enzyme mRNA expression, transcript of approximately 2 kb length dominant
-
mAGPAT1, mAGPAT2, mAGPAT3, mAGPAT4 barely detectable, mAGPAT5 expressed at high levels, mRNA expression of cardiac mAGPAT3 is regulated by activation of peroxisome-proliferator-activated receptors
-
analysis of enzyme mRNA expression, transcript of approximately 2 kb length dominant
-
mAGPAT1, mAGPAT2, mAGPAT3, mAGPAT4 is expressed at low levels, mAGPAT5 expressed at intermediate levels
-
mAGPAT1, mAGPAT2, mAGPAT3, mAGPAT4 barelry detectable, mAGPAT5 expressed at low levels
-
analysis of enzyme mRNA expression, transcript of approximately 2 kb length dominant
-
mAGPAT1, mAGPAT3, mAGPAT2 is undetectable, mAGPAT4 expressed at low levels, mAGPAT5 expressed at low levels
-
analysis of enzyme mRNA expression, transcript of approximately 2 kb length dominant
-
mAGPAT1, mAGPAT2, mAGPAT, mAGPAT4 expressed at intermediate levels, mAGPAT5 expressed at high levels
-
analysis of enzyme mRNA expression, transcript of approximately 1.3 kb length dominant
-
mAGPAT1, mAGPAT3, mAGPAT2 is undetectable, mAGPAT4 is expressed at low levels, mAGPAT5 expressed at low levels
-
analysis of enzyme mRNA expression, transcript of approximately 2 kb length dominant
additional information
C4B4E7
tissue distribution of LPAAT3 expression, overview
additional information
analysis of tissue distribution of AGPAT2. AGPAT2 expression is increased during adipocyte differentiation and mutations cause congenital generalised lipodystrophy (CGL) type 1
additional information
analysis of tissue distribution of AGPAT2. AGPAT2 expression is increased during adipocyte differentiation and mutations cause congenital generalised lipodystrophy (CGL) type 1
additional information
the mRNA for murine AGPAT1 is ubiquitously expressed, analysis of tissue distribution of AGPAT1
additional information
the mRNA for murine AGPAT1 is ubiquitously expressed, analysis of tissue distribution of AGPAT1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform AGPAT1 localizes to cytoskeletal components, particularly to areas of actin polymerization in myoblasts
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
C4B4E7
the enzyme provides an an alternative important possibility to produce phosphatidylinositol in the testis
physiological function
malfunction
metabolism
physiological function
physiological function
C4B4E7
isoform LPAAT3 is induced during germ cell maturation. Differentiation of mouse GC-2spd(ts) spermatocytes into spermatides up-regulates isoform LPAAT3 mRNA, increases the amount of polyunsaturated phospholipids, and shifts the specificity for the incorporation of docosahexaenoic acid toward phosphatidylcholine and phosphatidylethanolamine. Stable knockdown of LPAAT3 in GC-2spd(ts) cells significantly decreases microsomal LPAAT3 activity, reduces levels of polyunsaturated phosphatidylethanolamine species, and impairs cell proliferation/survival during geneticin selection
physiological function
C4B4E7
stable transfection of TM4 Sertoli cells with isoform LPAAT3-small hairpin RNA leads to decreases in arachidonoyl-, eicosapentaenoyl-, and docosapentaenoyl-containing phosphatidylcholine and linoleoyl-containing phosphatidylethanolamine, phosphatidylserine, and phosphatidylglycerol. Expression of murine LPAAT3 in Chinese hamster ovary K1 cells has essentially an opposite effect. The level of polyunsaturated phosphatidylcholine correlates with cellular levels of free docosapentaenoic acid and eicosapentaenoic acid in TM4 and Chinese hamster ovary K1 cells, respectively
malfunction
-
striking decreases in both the oxygen consumption rate and the extracellular acidification rate are observed in enzyme-deficient CD4+ T cells following CD3/CD28 stimulation indicating an inherent cellular defect in energy production. In addition, the spare respiratory capacity and the mitochondrial membrane potential of these CD4+T cells is significantly decreased
malfunction
-
enzyme-deficient mice develop widespread disturbances of metabolism, sperm development, and neurologic function resulting from disrupted phospholipid homeostasis. Enzyme-deficient mice have reduced body weight, total body fat, and plasma leptin level and show features of epilepsy. Neonatal enzyme-deficient mice have minor alterations in lipid synthesis and reduced plasma glucose levels. Enzyme-deficient males and females mice have reproductive abnormalities
malfunction
in enzyme AGPAT2 defiecient mice, reduces TG synthesis and increased lyso-PA channeling into phospholipids is observed. In Agpat2-/- mouse liver, hepatic steatosis is driven by increased fatty acid synthesis and diversion of lyso-PA to TG and phospholipids by a mechanism independent of monoacylglycerol acyltransferase 1 (MGAT1) activity. The increase in phospholipid synthesis might be due to an alternate AGPAT-dependent pathway
metabolism
the enzyme specifically supports synthesis of brain phosphatidylinositol, phosphatidylcholine, and phosphatidylethanolamine
metabolism
the successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, glycerol-3-phosphate biosynthetic pathway, overview. Substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids
physiological function
expression of isoform CGI-58 in fibroblasts from humans with Chanarin-Dorfman increases the incorporation of fatty acids released from the lipolysis of stored triacylglycerols into phospholipids
physiological function
isoform AGPAT1 is involved in development of skeletal muscle. Small interference RNA-mediated knockdown of AGPAT1 expression prevents the induction of myogenin, and inhibits the expression of myosin heavy chain. This effect is rescued by transfection with AGPAT1 but not AGPAT2. The regulation of myogenesis by AGPAT1 is associated with alterations on actin cytoskeleton. AGPAT1 colocalizes AGPAT1 to areas of active actin polymerization. AGPAT1 overexpression is not associated with an increase in phosphatidic acid levels
physiological function
-
the enzyme is essential for the response to the increased metabolic demands associated with T cell activation
physiological function
while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs, suggesting a dual role in glycerolipid synthesis and remodeling
physiological function
while isozymes AGPAT1 and 2 show strict acyl acceptor specificity for lysophosphatidic acid, other isoforms utilize lyso-PC, -PE and -phosphatidylserine (PS) as acyl acceptors. Isozymes AGPAT3, AGPAT4, and AGPAT5 have LPAAT activity with oleoyl-CoA as the acyl donor, but also have LPLAT activity with a preference for polyunsaturated acyl-CoAs, suggesting a dual role in glycerolipid synthesis and remodeling. AGPAT2 plays a critical, non-redundant role in adipogenesis related to triglyceride (TG) synthesis and/or provision of phosphatidic acid (PA) for differentiation-dependent signaling pathways
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). PLCC_MOUSE
376
3
43296
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
C4B4E7
x * 43300, about, sequence calculation, x * 37000, about, recombinant FLAg-tagged enzyme, SDS-PAGE
43300
C4B4E7
x * 43300, about, sequence calculation, x * 37000, about, recombinant FLAg-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
C4B4E7
x * 43300, about, sequence calculation, x * 37000, about, recombinant FLAg-tagged enzyme, SDS-PAGE
additional information
additional information
-
the CGI-58 carboxyl terminus includes a highly conserved consensus sequence, HXXXXD, required for acyltransferase activity
additional information
the CGI-58 carboxyl terminus includes a highly conserved consensus sequence, HXXXXD, required for acyltransferase activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
recombinant expression of murine CGI-58 in fibroblasts from humans with Chanarin-Dorfman syndrome increases the incorporation of radiolabeled fatty acids released from the lipolysis of stored triacylglycerols into phospholipids
additional information
recombinant expression of murine CGI-58 in fibroblasts from humans with Chanarin-Dorfman syndrome increases the incorporation of radiolabeled fatty acids released from the lipolysis of stored triacylglycerols into phospholipids
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
LPAAT3, phylogenetic analysis, expression of the FLAG-tagged enzyme in CHO-K1 cells
C4B4E7
expression in Escherichia coli JC201, a mutant strain deficient in the enzyme activity
-
gene AGPAT8, DNA and amino acid sequence determination and analysis, localization on chromosome 17, genetic structure, expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the enzyme in the testis increases significantly in an age-dependent manner, which is regulated by induction through beta-estradiol, in TM4 cells
C4B4E7
isoform LPAAT3 is induced during germ cell maturation. Differentiation of mouse GC-2spd(ts) spermatocytes into spermatides up-regulates isoform LPAAT3 mRNA, increases the amount of polyunsaturated phospholipids, and shifts the specificity for the incorporation of docosahexaenoic acid toward phosphatidylcholine and phosphatidylethanolamine
C4B4E7
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
expression of isoform CGI-58 in fibroblasts from humans with Chanarin-Dorfman increases the incorporation of fatty acids released from the lipolysis of stored triacylglycerols into phospholipids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kume, K.; Shimizu, T.
cDNA cloning and expression of murine 1-acyl-sn-glycerol-3-phosphate acyltransferase
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237
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1997
Mus musculus
Yamashita, A.; Kawagishi, N.; Miyashita, T.; Nagatsuka, T.; Sugiura, T.; Kume, K.; Shimizu, T.; Waku, K.
ATP-independent fatty acyl-coenzyme A synthesis from phospholipid: coenzyme A-dependent transacylation activity toward lysophosphatidic acid catalyzed by acyl-coenzyme A:lysophosphatidic acid acyltransferase
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276
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2001
Mus musculus
Lu, B.; Jiang, Y.J.; Zhou, Y.; Xu, F.Y.; Hatch, G.M.; Choy, P.C.
Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart
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385
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2005
Mus musculus
Agarwal, A.K.; Barnes, R.I.; Garg, A.
Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity
Arch. Biochem. Biophys.
449
64-76
2006
Homo sapiens, Mus musculus
Lu, B.; Jiang, Y.J.; Man, M.Q.; Brown, B.; Elias, P.M.; Feingold, K.R.
Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis
J. Lipid Res.
46
2448-2457
2005
Mus musculus
Yuki, K.; Shindou, H.; Hishikawa, D.; Shimizu, T.
Characterization of mouse lysophosphatidic acid acyltransferase 3: an enzyme with dual functions in the testis
J. Lipid Res.
50
860-869
2009
Mus musculus (C4B4E7), Mus musculus, Mus musculus C57/BL6J (C4B4E7)
Montero-Moran, G.; Caviglia, J.M.; McMahon, D.; Rothenberg, A.; Subramanian, V.; Xu, Z.; Lara-Gonzalez, S.; Storch, J.; Carman, G.M.; Brasaemle, D.L.
CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid acyltransferase
J. Lipid Res.
51
709-719
2009
Homo sapiens, Mus musculus, Mus musculus (Q9DBL9)
Subauste, A.R.; Elliott, B.; Das, A.K.; Burant, C.F.
A role for 1-acylglycerol-3-phosphate-O-acyltransferase-1 in myoblast differentiation
Differentiation
80
140-146
2010
Mus musculus (O35083)
Koeberle, A.; Shindou, H.; Harayama, T.; Shimizu, T.
Role of lysophosphatidic acid acyltransferase 3 for the supply of highly polyunsaturated fatty acids in TM4 Sertoli cells
FASEB J.
24
4929-4938
2010
Mus musculus (C4B4E7), Mus musculus
Koeberle, A.; Shindou, H.; Harayama, T.; Yuki, K.; Shimizu, T.
Polyunsaturated fatty acids are incorporated into maturating male mouse germ cells by lysophosphatidic acid acyltransferase 3
FASEB J.
26
169-180
2012
Mus musculus (C4B4E7), Mus musculus
Eto, M.; Shindou, H.; Shimizu, T.
A novel lysophosphatidic acid acyltransferase enzyme (LPAAT4) with a possible role for incorporating docosahexaenoic acid into brain glycerophospholipids
Biochem. Biophys. Res. Commun.
443
718-724
2014
Mus musculus (Q8K4X7), Mus musculus
Faris, R.; Fan, Y.; De Angulo, A.; Chapkin, R.; Degraffenried, L.; Jolly, C.
Mitochondrial glycerol-3-phosphate acyltransferase-1 is essential for murine CD4+ T cell metabolic activation
Biochim. Biophys. Acta
1841
1475-1482
2014
Mus musculus
-
Bradley, R.M.; Marvyn, P.M.; Aristizabal Henao, J.J.; Mardian, E.B.; George, S.; Aucoin, M.G.; Stark, K.D.; Duncan, R.E.
Acylglycerophosphate acyltransferase 4 (AGPAT4) is a mitochondrial lysophosphatidic acid acyltransferase that regulates brain phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol levels
Biochim. Biophys. Acta
1851
1566-1576
2015
Mus musculus (Q8K4X7), Mus musculus
Lin, S.; Ikegami, M.; Moon, C.; Naren, A.P.; Shannon, J.M.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) specifically interacts with phospholipid transfer protein starD10 to facilitate surfactant phospholipid trafficking in alveolar type II cells
J. Biol. Chem.
290
18559-18574
2015
Mus musculus (Q3TFD2)
Lee, J.; Ridgway, N.
Substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids
Biochim. Biophys. Acta
1865
158438-158448
2020
Homo sapiens (O15120), Homo sapiens (Q99943), Homo sapiens (Q9NRZ5), Homo sapiens (Q9NRZ7), Homo sapiens (Q9NUQ2), Mus musculus (O35083), Mus musculus (Q8K3K7)
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