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EC Tree
IUBMB 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.
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae 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
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3-glycerophosphate acyltransferase
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ACP:sn-glycerol-3-phosphate acyltransferase
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acyltransferase, glycerol phosphate
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alpha-glycerophosphate acyltransferase
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glycerol 3-phosphate acyltransferase
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glycerol phosphate acyltransferase
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glycerol phosphate transacylase
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glycerol-3-phosphate acyltransferase 1
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glycerophosphate acyltransferase
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glycerophosphate transacylase
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Sn-glycerol 3-phosphate acyltransferase
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additional information
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enzyme may be identical with EC 2.3.1.42
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Acyl group transfer
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-, -, -, -, -, -, -, -, -
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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.
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acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
enzyme has both 3-glycerophosphate acyltransferase and dihydroxyacetone phosphate acyltransferase activity
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?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
low activity
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?
palmitoleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoleoyl-sn-glycerol 3-phosphate
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-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
preferred acyl-donor
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?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
low activity
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?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
myristoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-myristoyl-sn-glycerol 3-phosphate
n-dodecanoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-n-dodecanoyl-sn-glycerol 3-phosphate
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i.e. lauroyl-CoA, poor substrate
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?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
palmitoleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoleoyl-sn-glycerol 3-phosphate
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-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
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broad specificity
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?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
enzyme has both 3-glycerophosphate acyltransferase and dihydroxyacetone phosphate acyltransferase activity
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?
acyl-CoA + sn-glycerol 3-phosphate
CoA + 1-acyl-sn-glycerol 3-phosphate
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enzyme has both 3-glycerophosphate acyltransferase and dihydroxyacetonephosphate acyltransferase activity
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?
myristoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-myristoyl-sn-glycerol 3-phosphate
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i.e. tetradecanoyl-CoA
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?
myristoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-myristoyl-sn-glycerol 3-phosphate
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i.e. tetradecanoyl-CoA
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?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
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?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
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?
oleoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-oleoyl-sn-glycerol 3-phosphate
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-
?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
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-
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?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
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?
palmitoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-palmitoyl-sn-glycerol 3-phosphate
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i.e. n-hexadecanoyl-CoA, best substrate
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?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
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-
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?
stearoyl-CoA + sn-glycerol 3-phosphate
CoA + 1-stearoyl-sn-glycerol 3-phosphate
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-
?
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deoxycholate
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above 0.35 mg/ml
dihydroxyacetone phosphate
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N-ethylmaleimide
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0.4 mM, 60% inhibition after 10 min
Triton X-100
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strong, above 0.15 mg/ml
Trypsin
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0.06 mg/ml, 80% inhibition after 10 min
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oleate
presence of oleate induces dephosphorylation of isoform Gat1p as well as an increment in its levels. In presence of oleate, Gat1p crescent structures are formed which are connected with the endoplasmic reticulum and are intimately associated with lipid particles
Triton X-100
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i.e. octylphenoxy polyethoxyethanol, slight stimulation at 0.1 mg/ml
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0.03
sn-glycerol 3-phosphate
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-
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0.54
dihydroxyacetone phosphate
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-
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7
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50% of maximal activity at pH 7.4
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6.6 - 8.9
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maximal activity at pH 6.6, approx. 30% of maximal activity at pH 8.9
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Gat2p
SwissProt
brenda
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brenda
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brenda
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subcellular localization of Gat1p and Gat2p are compared using fluorescence microscopy and subcellular fractionation using equilibrium density gradients. Gat1p and Gat2p overlap mostly in their localization and are microsomal GPATs, localized to both perinuclear and cortical endoplasmic reticula in actively proliferating cells
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brenda
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malfunction
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loss of function of Gat1p and Gat2p is masked by the compensatory effect of their redundant partner. The complete lack of GPAT results in cell death, with multibudded cells containing divided nuclei
physiological function
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overexpression Gat1p in the absence of endogenous GPATs results in elongated cells with a normal cortical edoplasmic reticulum positioned underneath the plasma membrane, while excess Gat2p results in larger and round cells with an irregular layout of membranes, with pronounced invaginations also affecting the plasma membrane morphology
physiological function
yeast strains lacking isoform Gat1p are sensitive to oleate and fail to accumulate lipid particles induced by this unsaturated fatty acid
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phosphoprotein
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phosphoprotein
presence of oleate induces dephosphorylation of isoform Gat1p
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-15°C, 3-5 mg/ml protein, membrane preparation, at least 2 months
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expression in Escherichia coli
expression in Escherichia coli
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presence of oleate induces dephosphorylation of isoform Gat1p as well as an increment in its levels
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Schlossman, D.M.; Bell, R.M.
Glycerolipid biosynthesis in Saccharomyces cerevisiae: sn-glycerol-3-phosphate and dihydroxyacetone phosphate acyltransferase activities
J. Bacteriol.
133
1368-1376
1978
Saccharomyces cerevisiae
brenda
Yamada, K.; Okuyama, H.; Endo, Y.; Ikezawa, H.
Acyltransferase systems involved in phospholipid metabolism in Saccharomyces cerevisiae
Arch. Biochem. Biophys.
183
281-289
1977
Saccharomyces cerevisiae, Saccharomyces cerevisiae OC-2
brenda
Zheng, Z.; Zou, J.
The initial step of the glycerolipid pathway: identification of glycerol 3-phosphate/dihydroxyacetone phosphate dual substrate acyltransferases in Saccharomyces cerevisiae
J. Biol. Chem.
276
41710-41716
2001
Saccharomyces cerevisiae (P32784), Saccharomyces cerevisiae (P36148), Saccharomyces cerevisiae
brenda
Bratschi, M.W.; Burrowes, D.P.; Kulaga, A.; Cheung, J.F.; Alvarez, A.L.; Kearley, J.; Zaremberg, V.
Glycerol-3-phosphate acyltransferases gat1p and gat2p are microsomal phosphoproteins with differential contributions to polarized cell growth
Eukaryot. Cell
8
1184-1196
2009
Saccharomyces cerevisiae
brenda
Marr, N.; Foglia, J.; Terebiznik, M.; Athenstaedt, K.; Zaremberg, V.
Controlling lipid fluxes at glycerol-3-phosphate acyltransferase step in yeast: unique contribution of Gat1p to oleic acid-induced lipid particle formation
J. Biol. Chem.
287
10251-10264
2012
Saccharomyces cerevisiae (P36148), Saccharomyces cerevisiae
brenda
Transporter Classification Database (TCDB):
9.B.31.1.1