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Information on EC 2.3.1.15 - glycerol-3-phosphate 1-O-acyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q5XF03
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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.
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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: Arabidopsis thaliana
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
3-glycerophosphate acyltransferase
-
-
-
-
ACP:sn-glycerol-3-phosphate acyltransferase
-
-
-
-
acyltransferase, glycerol phosphate
-
-
-
-
alpha-glycerophosphate acyltransferase
-
-
-
-
AT1G02390
glycerol 3-phosphate acyltransferase
-
-
-
-
glycerol phosphate acyltransferase
-
-
-
-
glycerol phosphate transacylase
-
-
-
-
glycerol-3-phosphate acyltransferase
glycerophosphate acyltransferase
-
-
-
-
glycerophosphate transacylase
-
-
-
-
Sn-glycerol 3-phosphate acyltransferase
-
-
-
-
sn-glycerol-3-phosphate acyltransferase
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-dicarboxylic acyl-sn-glycerol 3-phosphate
-
-
-
?
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-dicarboxylic acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-omega-hydroxy-acyl-sn-glycerol 3-phosphate
-
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-omega-hydroxy-acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-dicarboxylic acyl-sn-glycerol 3-phosphate
-
-
-
?
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-dicarboxylic acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
oleoyl-[acyl-carrier protein] + sn-glycerol 3-phosphate
acyl-carrier protein + 1-oleoyl-sn-glycerol 3-phosphate
-
oleoyl-[acyl-carrier-protein] is preferred over palmitoyl-[acyl-carrier-protein]
-
?
omega-hydroxy acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-omega-hydroxy acyl-sn-glycerol 3-phosphate
-
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-omega-hydroxy-acyl-sn-glycerol 3-phosphate
-
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-omega-hydroxy-acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
-
-
?
palmitoyl-[acyl-carrier protein] + sn-glycerol 3-phosphate
acyl-carrier protein + 1-palmitoyl-sn-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
-
-
-
?
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
-
preferred over palmitoyl-CoA with a ratio of approx. 3:1
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
preferred over palmitoyl-CoA
-
?
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
omega-hydroxy-acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA is the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
acyl-CoA ist the preferred substrate compared to dicarboxylic acyl-CoA. The isozyme shows a regiospecificity that prefers sn-1 before sn-2
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
dicarboxylic acyl-CoA is the preferred substrate. The isozyme shows a regiospecificity that is equally sn-2 and sn-1
-
-
-
additional information
?
-
regiospecificity of GPAT9, the majority of the acylation reactions catalyzed by this enzyme takes place at the sn-1 position rather than the sn-2 position (5.3:1 ratio)
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
additional information
?
-
the isozyme prefers very-long-chain (C22) acyl-Co as substrate compared to dicarboxylic acyl-CoA and omega-hydroxy acyl-CoA. The isozyme shows a regiospecificity that prefers sn-2 before sn-1
-
-
-
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
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-dicarboxylic acyl-sn-glycerol 3-phosphate
-
-
-
?
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-dicarboxylic acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-omega-hydroxy-acyl-sn-glycerol 3-phosphate
-
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-omega-hydroxy-acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-dicarboxylic acyl-sn-glycerol 3-phosphate
-
-
-
?
dicarboxylic acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-dicarboxylic acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
omega-hydroxy acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-omega-hydroxy acyl-sn-glycerol 3-phosphate
-
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-omega-hydroxy-acyl-sn-glycerol 3-phosphate
-
-
-
?
omega-hydroxy-acyl-CoA + sn-glycerol 3-phosphate
CoA + 2-omega-hydroxy-acyl-sn-glycerol 3-phosphate
reaction of EC 2.3.1.198, glycerol-3-phosphate 2-O-acyltransferase
-
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-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
-
-
-
?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
synthesis of unsaturated fatty acid and double bond index (DBI) of phosphatidylglycerol of plants are inhibited by salt stress
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
GPAT9 is constitutively expressed. The expression pattern is relatively broad. Comparable levels of GPAT9 expression are noted in the majority of tissues tested, including seedlings, rosette and cauline leaves (28 DAP), stems, roots, floral buds, open flowers, pollen, and siliques/seeds/embryos at various developmental stages. The highest levels of expression appears to be evident in leaves and developing siliques [at about 9 d after flowering (DAF)]
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
differential permeabilization experiments indicate that their N- and C-termini are oriented towards the cytosol. GPAT8 possesses a divergent type of dilysine motif -KK-COOH which only functions effectively when additional upstream residues are included to provide the proper protein context
-
differential permeabilization experiments indicate that their N- and C-termini are oriented towards the cytosol. GPAT9 possesses a hydrophobic pentapeptide motif (-f-X-X-K/R/D/E-f-, where f are large hydrophobic amino acid residues)
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT8 plays a role in cutin biosynthesis (functionally redundant with GPAT4)
malfunction
metabolism
physiological function
malfunction
a knockout mutant of isoform GPAT9 demonstrates both male and female gametophytic lethality phenotypes
malfunction
alteration of constitutive GPAT9 expression has no obvious effects on surface lipid biosynthesis. But overexpression and downregulation of GPAT9 in Arabidopsis thaliana results in changes in seed size, as well as seed oil content and composition. Altering the constitutive expression of GPAT9 in Arabidopsis enhances production of lipid droplets in pollen grains. Knockout of gpat9 has been shown to result in a male gametophytic lethality phenotype
malfunction
GPAT2 mutant seeds show reduced germination rates and root lengths compared to wild-type in presence of 50-150 mM salt. Overexpression of glycerol-3-phosphate acyltransferase from Suaeda salsa improves salt tolerance in Arabidopsis thaliana deficient in GPAT2. In the seedling stage, chlorophyll content, the photochemical efficiency of PSII, PSI oxidoreductive activity (1I/Io), and the unsaturated fatty acid content of PG decrease less in overexpressing strains and more in mutant strains than that in wild-type under salt stress. The overexpression of SsGPAT alleviates the photoinhibition of PSII and PSI under salt stress by improving the unsaturated fatty acid content of phosphatidylglycerol (PG)
metabolism
glycerol-3-phosphate acyltransferase (GPAT) is the first acyl esterifying enzyme in phosphatidylglycerol (PG) synthesis process
metabolism
the preference of GPAT9 for acyl-CoA as its substrate, and its sn-1 regio-specificity, provide support that it plays an important role in the Kennedy pathway of glycerolipid biosynthesis
physiological function
-
the knockout mutant causes a massive reduction in seed production. The ablation of enzyme function causes defective tapetum development with reduced endoplasmic reticulum profiles in the tapetum, which largely lead to the abortion of pollen grains and defective pollen wall formation. Pollen germination and pollen tube elongation are affected in the mutant plants. Isoforms GPAT6 and GPAT1 make joint effects on the release of microspores from tetrads and stamen filament elongation
physiological function
the enzyme isoform GPAT-9 plays a role in essential membrane lipid synthesis. The enzyme is responsible for plant membrane lipid and oil biosynthesis
physiological function
enzyme GPAT9 has a role for GPAT9 in seed oil biosynthesis and contributes to the biosynthesis of both polar lipids and triacylglycerol (TAG) in developing leaves, as well as lipid droplet production in developing pollen grains. GPAT9 exhibits sn-1 acyltransferase activity with high specificity for acyl-coenzyme A, thus providing further evidence that this GPAT is involved in storage lipid biosynthesis
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids in leaves, pollen, and seeds
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT1 plays a role in cutin biosynthesis, dephosphorylation, and pollen sperm cell differentiation
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT2 plays a role in cutin biosynthesis and dephosphorylation
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT3 plays a role in cutin biosynthesis, dephosphorylation, and other metabolic processes
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT5 plays a role in root and seed coat suberin synthesis
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT7 plays a role in suberin biosynthesis as a response to wounding in aerial tissues
physiological function
the enzyme transfers the acyl moiety from an acyl-coenzyme A (CoA) donor (or acyl-acyl carrier protein [ACP] in plastids) to the sn-1 position of a glycerol-3-phosphate (G3P) molecule, yielding 1-acylglycerol-3-phosphate (or lysophosphatidic acid, LPA)
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). GPAT8_ARATH
500
2
55867
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of a T-DNA insertion mutant strain of GPAT2, determination of chlorophyll content and fatty acids composition of phosphatidylglycerol (PG) in Arabidopsis thaliana GPAT6 mutant line, overview. In the seedling stage, chlorophyll content, the photochemical efficiency of PSII, PSI oxidoreductive activity (1I/Io), and the unsaturated fatty acid content of PG decrease less in overexpressing strains and more in mutant strains than that in wild-type under salt stress. Overexpression of glycerol-3-phosphate acyltransferase from Suaeda salsa improves salt tolerance in Arabidopsis thaliana deficient in GPAT2. The overexpression of SsGPAT alleviates the photoinhibition of PSII and PSI under salt stress by improving the unsaturated fatty acid content of PG
additional information
generation of two GPAT9 overexpression vectors, i.e. constitutive (GPAT9-OE) and seed-specific (GPAT9-SS-OE) vectors, respectively, and of two GPAT9 RNAi vectors, i.e. constitutive (GPAT9-RNAi) and seed-specific (GPAT9-SS-RNAi) vectors, respectively. To generate GPAT9 overexpression constructs, the GPAT9 coding sequence is inserted between the constitutive tobacco tCUP3 promoter and Pisum sativum ribulose-1,5-bisphosphate carboxylase transcriptional terminator (rbcS-t) to generate the GPAT9-OE vector, or between the seed-specific Brassica napus Napin promoter and rbcS-t transcriptional terminator to produce the GPAT9-SS-OE vector. The GPAT9 RNAi fragments are inserted in opposite orientations between the constitutive tCUP3 promoter and intronic spacer from the pHannibal plasmid, and rbcS-t transcriptional terminator and intronic spacer, respectively. These same sense and antisense GPAT9 fragments are also inserted between the seed-specific Phaseolus vulgaris beta-phaseolin promoter and pHannibal intronic spacer, and the beta-phaseolin transcriptional terminator and intronic spacer, respectively, in a pPZP-RSC1 background. Overexpression and down-regulation of GPAT9 in Arabidopsis thaliana results in changes in seed size, as well as seed oil content and composition, phenotypes, overview. Overexpression of GPAT9 in GPAT9-OE lines results in increased seed oil content, downregulation of this gene in GPAT9-RNAi lines yields significant decreases in seed oil content. No significant differences are noted in seed yields between either T3 homozygous GPAT9-OE and wild-type lines, or GPAT9-RNAi and wild-type. Altering the constitutive expression of GPAT9 in Arabidopsis enhances production of lipid droplets in pollen grains
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a myc-epitope-tagged fusion protein in Tobacco suspension cultured cells
expressed as a myc-epitope-tagged fusion protein in Tobacco suspension cultured cells
gene GPAT2, sequence comparisons and phylogenetic tree, quantitative real-time PCR enzyme expression analysis
gene GPAT9, recombinant expression in Saccharomyces cerevisiae strain gat1DELTA (Matalpha, his3C1, leu2C0, lys2C0, ura3C0, YKR067w::kanMX4), quantitative real-time RT-PCR analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murata, N.; Tasaka, Y.
Glycerol-3-phosphate acyltransferase in plants
Biochim. Biophys. Acta
1348
10-16
1997
Arabidopsis thaliana, Persea americana, Ricinus communis, Cucumis sativus, Cucurbita moschata, Phaseolus vulgaris, Pisum sativum, Solanum tuberosum, Spinacia oleracea
Slabas, A.R.; Simon, W.R.; Schierer, T.; Kroon, J.; Fawcett, T.; Hayman, M.; Gilroy, J.; Nishida, I.; Murata, N.; Rafferty, J.; Turnbull, A.; Rice, D.
Plant glycerol-3-phosphate-1-acyltransferase (GPAT): structure selectivity studies
Biochem. Soc. Trans.
28
677-679
2000
Arabidopsis thaliana, Cucurbita moschata, Elaeis guineensis, Pisum sativum, Spinacia oleracea
Hayman, M.W.; Fawcett, T.; Schierer, T.F.; Simon, J.W.; Kroon, J.T.M.; Gilroy, J.S.; Rice, D.W.; Rafferty, J.; Turnbull, A.P.; Sedelnikova, S.E.; Slabas, A.R.
Mutagenesis of squash (Cucurbita moschata) glycerol-3-phosphate acyltransferase (GPAT) to produce an enzyme with altered substrate selectivity
Biochem. Soc. Trans.
28
680-681
2000
Arabidopsis thaliana, Cucurbita moschata
Slabas, A.R.; Kroon, J.T.M.; Scheirer, T.P.; Gilroy, J.S.; Hayman, M.; Rice, D.W.; Turnbull, A.P.; Rafferty, J.B.; Fawcett, T.; Simon, W.J.
Squash Glycerol-3-phosphate (1)-Acyltransferase. Alteration of substrate selectivity and identification of arginine and lysine residues important in catalytic activity
J. Biol. Chem.
277
43918-43923
2002
Arabidopsis thaliana, Cucurbita moschata, Elaeis guineensis
Hayman, M.W.; Fawcett, T.; Slabas, A.R.
Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata)
FEBS Lett.
514
281-284
2002
Arabidopsis thaliana, Cucurbita moschata
Gidda, S.K.; Shockey, J.M.; Rothstein, S.J.; Dyer, J.M.; Mullen, R.T.
Arabidopsis thaliana GPAT8 and GPAT9 are localized to the ER and possess distinct ER retrieval signals: functional divergence of the dilysine ER retrieval motif in plant cells
Plant Physiol. Biochem.
47
867-879
2009
Arabidopsis thaliana (Q5XF03), Arabidopsis thaliana (Q8GWG0), Arabidopsis thaliana
Li, X.C.; Zhu, J.; Yang, J.; Zhang, G.R.; Xing, W.F.; Zhang, S.; Yang, Z.N.
Glycerol-3-phosphate acyltransferase 6 (GPAT6) is important for tapetum development in Arabidopsis and plays multiple roles in plant fertility
Mol. Plant
5
131-142
2012
Arabidopsis thaliana
Shockey, J.; Regmi, A.; Cotton, K.; Adhikari, N.; Browse, J.; Bates, P.D.
Identification of Arabidopsis GPAT9 (At5g60620) as an essential gene involved in triacylglycerol biosynthesis
Plant Physiol.
170
163-179
2016
Arabidopsis thaliana (Q8GWG0)
Sui, N.; Tian, S.; Wang, W.; Wang, M.; Fan, H.
Overexpression of glycerol-3-phosphate acyltransferase from Suaeda salsa improves salt tolerance in Arabidopsis
Front. Plant Sci.
8
1337
2017
Suaeda salsa, Arabidopsis thaliana (Q9FZ22), Arabidopsis thaliana Col-0 (Q9FZ22)
Singer, S.D.; Chen, G.; Mietkiewska, E.; Tomasi, P.; Jayawardhane, K.; Dyer, J.M.; Weselake, R.J.
Arabidopsis GPAT9 contributes to synthesis of intracellular glycerolipids but not surface lipids
J. Exp. Bot.
67
4627-4638
2016
Arabidopsis thaliana (Q8GWG0)
Jayawardhane, K.N.; Singer, S.D.; Weselake, R.J.; Chen, G.
Plant sn-glycerol-3-phosphate acyltransferases biocatalysts involved in the biosynthesis of intracellular and extracellular lipids
Lipids
53
469-480
2018
Arabidopsis thaliana (Q5XF03), Arabidopsis thaliana (Q8GWG0), Arabidopsis thaliana (Q9CAY3), Arabidopsis thaliana (Q9FZ22), Arabidopsis thaliana (Q9LHS7), Arabidopsis thaliana (Q9SHJ5), Arabidopsis thaliana (Q9SYJ2)
EXTERNAL LINKS (specific for EC-Number 2.3.1.15)
Transporter Classification Database (TCDB): 9.B.31.1.1
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