The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation.
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SYSTEMATIC NAME
IUBMB Comments
an acyl-[acyl-carrier protein]:phosphate acyltransferase
The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation.
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Peroxisomal Disorders
Prenatal diagnosis of Zellweger syndrome by measurement of very long chain fatty acid (C26:0) beta-oxidation in cultured chorionic villous fibroblasts: implications for early diagnosis of other peroxisomal disorders.
Prenatal diagnosis of Zellweger syndrome by measurement of very long chain fatty acid (C26:0) beta-oxidation in cultured chorionic villous fibroblasts: implications for early diagnosis of other peroxisomal disorders.
Prenatal diagnosis of Zellweger syndrome by measurement of very long chain fatty acid (C26:0) beta-oxidation in cultured chorionic villous fibroblasts: implications for early diagnosis of other peroxisomal disorders.
the enzyme is uniformly distributed on the membrane of most cells, but occasionally appears as membrane foci as well. Foci and homogenous patterns seem freely interconvertible but the prevalence of the uniform staining suggests that PlsX does not need to localize to specific sites to function correctly. PlsX's foci show no obvious periodicity of localization and do not colocalize with the divisome
the enzyme is uniformly distributed on the membrane of most cells, but occasionally appears as membrane foci as well. Foci and homogenous patterns seem freely interconvertible but the prevalence of the uniform staining suggests that PlsX does not need to localize to specific sites to function correctly. PlsX's foci show no obvious periodicity of localization and do not colocalize with the divisome
the enzyme is uniformly distributed on the membrane of most cells, but occasionally appears as membrane foci as well. Foci and homogenous patterns seem freely interconvertible but the prevalence of the uniform staining suggests that PlsX does not need to localize to specific sites to function correctly. PlsX's foci show no obvious periodicity of localization and do not colocalize with the divisome
repression of slr1510 increases octadecanol productivity threefold over the base strain. Accumulation of fatty alcohols impairs growth, alters the membrane composition, and causes a build-up of reactive oxygen species
PlsX is a central enzyme of phospholipid synthesis in bacteria, converting acyl-ACP to acyl-phosphate on the pathway to phosphatidic acid formation. PlsX plays a key role in the coordination of fatty acid and phospholipid synthesis
PlsX is a central enzyme of phospholipid synthesis in bacteria, converting acyl-ACP to acyl-phosphate on the pathway to phosphatidic acid formation. PlsX plays a key role in the coordination of fatty acid and phospholipid synthesis
substrate recognition and catalytic mechanism of phosphate acyltransferase PlsX, docking simulation, detailed overview. Conservation of potential active-site residues, sequence comparisons. The suspected ACP docking site is formed by Arg73 and Arg120
substrate recognition and catalytic mechanism of phosphate acyltransferase PlsX, docking simulation, detailed overview. Conservation of potential active-site residues, sequence comparisons. The suspected ACP docking site is formed by Arg73 and Arg120
substrate recognition and catalytic mechanism of phosphate acyltransferase PlsX, docking simulation, detailed overview. Conservation of potential active-site residues, sequence comparisons. The suspected ACP docking site is formed by Arg73 and Arg120
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion in hanging drops by mixing 0.001 ml of the protein solution (15 mg/ml) with 0.001 ml of 0.1 M HEPES pH 7.5, 15% Ethanol, 0.2 M MgCl2, and equilibrated at 295 K over 0.5 ml of this solution. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 62.36 A, b = 82.42 A, c = 147.24 A, a = b = c = 90°
site-directed mutagenesis, the mutation causes the greatest kcat decrease by more than 10fold and increases KM by 4.4 and 2.6fold for palmitoyl-ACP and phosphate, respectively
site-directed mutagenesis, most of the catalytic activity of mutant N229A is recovered with a 2.2fold KM increase for palmitoyl-ACP when glutamine is introduced into the mutated position in N229Q
site-directed mutagenesis, the catalytic activity of the negative control mutant protein R114A is essentially the same compared to wild-type enzyme for both substrates
site-directed mutagenesis, the mutation causes a significant 3.3fold increase in KM for palmitoyl-ACP without adverse effect on other kinetic constants
site-directed mutagenesis, the mutation causes a significant 2.5fold increase in KM for palmitoyl-ACP without adverse effect on other kinetic constants
site-directed mutagenesis, the mutation causes the greatest kcat decrease by more than 10fold and increases KM by 4.4 and 2.6fold for palmitoyl-ACP and phosphate, respectively
site-directed mutagenesis, the catalytic activity of the negative control mutant protein R114A is essentially the same compared to wild-type enzyme for both substrates
site-directed mutagenesis, the mutation causes a significant 2.5fold increase in KM for palmitoyl-ACP without adverse effect on other kinetic constants
Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX
Sastre, D.; Bisson-Filho, A.; de Mendoza, D.; Gueiros-Filho, F.
Revisiting the cell biology of the acyl-ACP Phosphate transacylase PlsX suggests that the phospholipid synthesis and cell division machineries are not coupled in Bacillus subtilis