A0A1V6KKT5 i.e. subunit PaaA, A0A125H2T4 i.e. subunit PaaB, A0A2N9CKU5 i.e. subunit PaaC, A0A088UAI6 i.e. subunit PaaD, and A0A7G6UV70 i.e. subunit PaaE
inhibition of quorum sensing by release of phenylacetic acid leads to attenuated virulence of the Burkholderia cenocepacia paaABCDE mutant. Burkholderia cenocepacia paaA and paaE mutants, in which the paaABCDE gene cluster is interrupted, are defective in PAA degradation and are attenuated for virulence in the nematode host model Caenorhabditis elegans. While the mutants of the PAA-CoA monooxygenase complex re attenuated for pathogenicity, mutants of the ring opening or beta-oxidation steps are not, possibly because some by-products are required for pathogenicity but not produced in DELTApaaABCDE. Phenotypes, overview
inhibition of quorum sensing by release of phenylacetic acid leads to attenuated virulence of the Burkholderia cenocepacia paaABCDE mutant. Burkholderia cenocepacia paaA and paaE mutants, in which the paaABCDE gene cluster is interrupted, are defective in PAA degradation and are attenuated for virulence in the nematode host model Caenorhabditis elegans. While the mutants of the PAA-CoA monooxygenase complex re attenuated for pathogenicity, mutants of the ring opening or beta-oxidation steps are not, possibly because some by-products are required for pathogenicity but not produced in DELTApaaABCDE. Phenotypes, overview
the phenylacetic acid degradation pathway of Burkholderia cenocepacia is active during cystic fibrosis-like conditions and is necessary for full pathogenicity of Burkholderia cenocepacia in nematode and rat infection models. Pathogenicity against Caenorhabditis elegans, increased with exogenous N-octanoyl-L-homoserine lactone
loss of PaaABCDE decreases virulence. Deletion of either ligase PaaK or PaaABCDE leads to higher levels of released phenylacetic acid but no differences in levels of internal accumulation compared to the wild-type level. Removal of PaaABCDE in a LuxIR-like quorum sensing system CepR mutant does not impact its attenuated phenotype
the phenylacetic acid degradation pathway of Burkholderia cenocepacia is active during cystic fibrosis-like conditions and is necessary for full pathogenicity of Burkholderia cenocepacia in nematode and rat infection models. Pathogenicity against Caenorhabditis elegans, increased with exogenous N-octanoyl-L-homoserine lactone
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in the absence of a bound ligand (with 100 mM N-(2-acetamido)-iminodiacetic acid pH 5.5) as well as in complexes with CoA, 3-hydroxybutyryl-CoA, benzoyl-CoA and phenylacetyl-CoA, using either 0.1 M PIPES pH 6.5, 15% (w/v) PEG 550 monomethyl ether or 0.1 M PIPES pH 6.5, 5% (v/v) 2-propanol, 5% (w/v) PEG 550 monomethyl ether
hanging drop vapor diffusion method, PaaAC with acetyl-CoA is crystallized in 0.1 M sodium citrate buffer, pH 5.5, and 15% (w/v) PEG 6000 (Fluka). Crystals of ligand-free PaaAC are obtained in 100 mM N-(2-acetamido)-iminodiacetic acid, pH 5.5
Burkholderia cenocepacia paaA and paaE mutants, in which the paaABCDE gene cluster is interrupted, are defective in PAA degradation and are attenuated for virulence in the nematode host model Caenorhabditis elegans. While the mutants of the PAA-CoA monooxygenase complex re attenuated for pathogenicity, mutants of the ring opening or beta-oxidation steps are not. henotypes, overview
Burkholderia cenocepacia paaA and paaE mutants, in which the paaABCDE gene cluster is interrupted, are defective in PAA degradation and are attenuated for virulence in the nematode host model Caenorhabditis elegans. While the mutants of the PAA-CoA monooxygenase complex re attenuated for pathogenicity, mutants of the ring opening or beta-oxidation steps are not. henotypes, overview
Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex