2.3.1.198: glycerol-3-phosphate 2-O-acyltransferase
This is an abbreviated version!
For detailed information about glycerol-3-phosphate 2-O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.198
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2.3.1.198
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cutin
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cuticle
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gpats
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acyl-coas
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brassica
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petals
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dicarboxylic
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land
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reticulum-localized
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floral
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glycerolipids
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waxes
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hero
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polyester
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anther
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erucic
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2-monoacylglycerol
- 2.3.1.198
- cutin
- cuticle
-
gpats
- acyl-coas
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brassica
-
petals
-
dicarboxylic
-
land
-
reticulum-localized
-
floral
- glycerolipids
- waxes
-
hero
-
polyester
-
anther
-
erucic
- 2-monoacylglycerol
Reaction
Synonyms
AT1G01610, At2g38110, AtGPAT4, AtGPAT6, glycerol-3-phosphate 2-O-acyltransferases, glycerol-3-phosphate acyltransferase, glycerol-3-phosphate acyltransferase 6, GPAT4, GPAT5, GPAT6, GPAT8, More, NbGPAT6a, PpGPAT2, PpGPAT4, SlGPAT6, SlGPAT6a, sn-2 acyltransferase, sn-2 GPAT, sn-2-GPAT, sn-glycerol-3-phosphate acyltransferase
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General Information
General Information on EC 2.3.1.198 - glycerol-3-phosphate 2-O-acyltransferase
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evolution
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occurrence of land-plant-specific glycerol-3-phosphate acyltransferases is essential for cuticle formation and gametophore development in Physcomitrella patens, sn-2 GPATs harboring both domains by gene recombination are critical to cuticle formation of early land plants. Phylogenetic analysis
malfunction
metabolism
physiological function
additional information
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a loss-of-function mutation in tomato SlGPAT6 results in increased susceptibility of leaves to Phytophthora infection, concomitant with changes in haustoria morphology. Modulation of GPAT6 expression alters the outer wall diameter of leaf epidermal cells. Tomato gpat6-a mutants have an impaired cell wall-cuticle continuum and fewer stomata, but show increased water loss
malfunction
glycerol content is strongly reduced in both stem and leaf cutin from all Arabidopsis thaliana mutants analyzed (gpat4/gpat8). Knocking out any of these genes individually, or as a pair (gpat4/gpat8), leads to large reductions in Arabidopsis thaliana cutin monomer loads, especially in the major monomer octadeca-6,9-diene-1,18-dioate (C18:2 DCA). sn-2-GPATs play pivotal roles in providing glycerol as a structural monomer for cutin through regiospecific sn-2 acylation of glycerol-3-phosphate. The double-knockout gpat4/gpat8 has an overall 60-70% reduction of aliphatic monomers in stem and leaf cutin, and the most pronounced decrease occurs in its major monomer, C18:2 dicarboxylic acyl-CoA (DCA)
malfunction
GPAT6 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 GPAT6. 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)
malfunction
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silencing of Nicotiana benthamiana NbGPAT6a increases leaf susceptibility to infection by the oomycetes Phytophthora infestans and Phytophthora palmivora, whereas overexpression of NbGPAT6a-GFP renders the leaves more resistant. Knockdown or knockout of GPAT6 renders leaves more susceptible to Phytophthora infection but more resistant to Bortrytis cinerea infection
malfunction
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targeted disruption of PpGPAT2 delays growth and gametophore development. Disruption of PpGPAT2 causes increased susceptibility to osmotic and salt stresses in Physcomitrella patens
malfunction
the G163R mutation in gpat6-a confers a loss of SlGPAT6-mediated GPAT activity leading to P23F12 glossy mutant line with with abnormal fruit cutin amounts/compositions and increased fruit brightness. Loss of SlGPAT6 function leads to altered expression of genes involved in cuticle and cell wall formation and remodeling
malfunction
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glycerol content is strongly reduced in both stem and leaf cutin from all Arabidopsis thaliana mutants analyzed (gpat4/gpat8). Knocking out any of these genes individually, or as a pair (gpat4/gpat8), leads to large reductions in Arabidopsis thaliana cutin monomer loads, especially in the major monomer octadeca-6,9-diene-1,18-dioate (C18:2 DCA). sn-2-GPATs play pivotal roles in providing glycerol as a structural monomer for cutin through regiospecific sn-2 acylation of glycerol-3-phosphate. The double-knockout gpat4/gpat8 has an overall 60-70% reduction of aliphatic monomers in stem and leaf cutin, and the most pronounced decrease occurs in its major monomer, C18:2 dicarboxylic acyl-CoA (DCA)
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malfunction
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GPAT6 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 GPAT6. 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)
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cutin biosynthesis involves the esterification of oxygenated 16- or 18-carbon fatty acids to glycerol through the action of glycerol-3-phosphate acyltransferases (GPAT4, GPAT6 and GPAT8). These enzymes have specificity for the second carbon of the glycerol (sn-2 position)
metabolism
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cutin biosynthesis involves the esterification of oxygenated 16- or 18-carbon fatty acids to glycerol through the action of glycerol-3-phosphate acyltransferases (GPAT4, GPAT6 and GPAT8). These enzymes have specificity for the second carbon of the glycerol (sn-2 position)
metabolism
isozymes GPAT4 and GPAT8 are glycerol-3-phosphate 2-O acyltransferases that catalyze the first step in leaf and stem cutin acylglycerol assembly
metabolism
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isozymes GPAT4 and GPAT8 are glycerol-3-phosphate 2-O acyltransferases that catalyze the first step in leaf and stem cutin acylglycerol assembly
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The enzyme is involved in cutin and suberin biosynthesis in plants. The common acyl monomer substrates (as CoA esters) are omega-hydroxy fatty acids (omega-OHFAs) and alpha,omega-dicarboxylic acids (DCAs). Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols (2-MAGs).
physiological function
The enzyme is involved in cutin and suberin biosynthesis in plants. The common acyl monomer substrates (as CoA esters) are omega-hydroxy fatty acids and alpha,omega-dicarboxylic acids. Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols (2-MAGs).
physiological function
H9XTI6; H9XTI4; H9XTI5
RNAi-mediated down-regulation of all Gpat4 homologues causes abnormal development of several reproductive organs and reduced seed set. Both pollen grains and developing embryo sacs of the downregulated Gpat4 lines are affected. The gpat4 mature embryos show decreased cutin content and altered monomer composition. The defective embryo development affects the oil body morphology, oil content, and fatty acid composition in Gpat4-lacking seeds
physiological function
glycerol-3-phosphate 2-O-acyltransferases (sn-2-GPATs) are essential for cutin biosynthesis and involved in cutin polymerization, cutin structures and compositions in plant tissues, detailed overview
physiological function
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glycerol-3-phosphate acyltransferase 6 controls filamentous pathogen interactions and cell wall properties of Nicotiana benthamiana leaf epidermis. Dual functionality of pathogen-inducible GPAT6 in controlling pathogen entry and cell wall properties affecting dehydration in leaves. Role for GPAT6-generated cutin monomers in influencing epidermal cell properties that are integral to leaf-microbe interactions and in limiting dehydration
physiological function
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glycerol-3-phosphate acyltransferase 6 controls filamentous pathogen interactions and cell wall properties of the tomato leaf epidermis. Dual functionality of pathogen-inducible GPAT6 in controlling pathogen entry and cell wall properties affecting dehydration in leaves. Role for GPAT6-generated cutin monomers in influencing epidermal cell properties that are integral to leaf-microbe interactions and in limiting dehydration
physiological function
glycerol-3-phosphate acyltransferase GPAT6 from tomato plays a central role in fruit cutin biosynthesis. Wild-type SlGPAT6 has the dual acyltransferase and phosphatase activities expected from a GPAT enzyme involved in cutin monomer biosynthesis
physiological function
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glycerol-3-phosphate acyltransferases is essential for cuticle formation and gametophore development in Physcomitrella patens. Glycerol-3-phosphate acyltransferase (GPAT) harboring bifunctional sn-2 acyltransferase/phosphatase activity produces 2-monoacylglycerol, a precursor for cutin synthesis. The cutin layer plays an important role in plant organ formation by providing organ boundaries. Floral organ fusion and permeable cuticle phenotypes of Arabidopsis thaliana mutant gpat6-2 petals are rescued to the wild-type by the expression of PpGPAT2 or PpGPAT4
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT4 plays a role in leaf and stem cutin biosynthetic processes and phospholipid biosynthetic process (functionally redundant with GPAT8)
physiological function
plant sn-glycerol-3-phosphate acyltransferases are biocatalysts involved in the biosynthesis of intracellular and extracellular lipids. Isozyme GPAT6 plays a role in flower cutin biosynthetic process, flower development, and the phospholipid biosynthetic process
physiological function
the enzyme is involved in cutin polymerization, cutin structures and compositions in plant tissues, detailed overview
physiological function
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glycerol-3-phosphate 2-O-acyltransferases (sn-2-GPATs) are essential for cutin biosynthesis and involved in cutin polymerization, cutin structures and compositions in plant tissues, detailed overview
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physiological function
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the enzyme is involved in cutin polymerization, cutin structures and compositions in plant tissues, detailed overview
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constitutive expression of NbGPAT6a renders leaves resistant to Phytophthora infection, NbGPAT6-mediated resistance is associated with longer-term leaf development processes. Modulating GPAT6 expression alters the thickness of the outer cell walls of the leaf epidermis
additional information
structural modeling of SlGPAT6, based on the Methanococcus jannaschii phospho-Ser phosphatase template and restricted to the N-terminal 17 to 207 amino acid region, generated in silico, revealing that the G-to-R amino acid substitution at position 163 is close to the cluster of residues that are essential for the catalytic activity and Mg2+ binding of GPAT6