6.2.1.30: phenylacetate-CoA ligase
This is an abbreviated version!
For detailed information about phenylacetate-CoA ligase, go to the full flat file.
Word Map on EC 6.2.1.30
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6.2.1.30
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phenylacetic
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penicillin
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chrysogenum
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putida
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ligases
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isopenicillin
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cenocepacia
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phenylglyoxylate
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benzoyl-coa
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denitrifying
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synthesis
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3-hydroxyphenylacetic
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phenylacetaldehyde
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analysis
- 6.2.1.30
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phenylacetic
- penicillin
- chrysogenum
- putida
- ligases
- isopenicillin
- cenocepacia
- phenylglyoxylate
- benzoyl-coa
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denitrifying
- synthesis
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3-hydroxyphenylacetic
- phenylacetaldehyde
- analysis
Reaction
Synonyms
EC 6.2.1.21, More, PA-CoA ligase, PAA-CoA ligase, PaaF2, PaaK1, PaaK2, PCL, phenyl/phenoxyacetic acid activating enzyme, phenyl/phenoxyacetyl-CoA-ligase, phenylacetyl CoA ligase, phenylacetyl-CoA ligase, phenylacetyl-CoA ligase (AMP-forming), phenylacetyl-coenzyme A ligase, Phl protein, phlB, PhlC, styrene-specific PA-CoA ligase, synthetase, phenacyl coenzyme A
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General Information
General Information on EC 6.2.1.30 - phenylacetate-CoA ligase
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evolution
metabolism
physiological function
additional information
PaaK1 and PaaK2 form a unique subgroup within the adenylate-forming enzyme superfamily
evolution
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PaaK1 and PaaK2 form a unique subgroup within the adenylate-forming enzyme superfamily
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PCL is essentially involved in the pathway of penicillin biosynthesis, overview. Conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental to antibiotic production
metabolism
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the enzyme catalyzes the second last step in penicillin N biosynthesis in microbodies, pathway overview and interorganelle intermediate transport
metabolism
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PCL is essentially involved in the pathway of penicillin biosynthesis, overview. Conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental to antibiotic production
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in a mutant lacking a 6-phophogluconate dehydratase and therefore unable to produce 2-keto-3-deoxy-6-phosphogluconate, phenylacetyl-CoA ligase activity is high, even in the presence of glucose plus phenylacetic acid. In wild-type, phenylacetyl-CoA ligase activity is low under these conditions
physiological function
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PCL is a side-chain precursor activation enzyme essentially involved in the pathway of penicillin biosynthesis, overview
physiological function
isozyme PaaK1 does not play a distinct role in pathogenesis of Burkholderia cenocepacia in Caenorhabditis elegans, although the catabolic pathway for phenylacetic acid degradation is a requirement for full pathogenesis
physiological function
the phenylacetic acid degradation pathway is the sole aerobic route for phenylacetic acid metabolism in bacteria and facilitates degradation of environmental pollutants such as styrene and ethylbenzene. The PAA pathway also is implicated in promoting Burkholderia cenocepacia infections in cystic fibrosis patients
physiological function
the phenylacetic acid degradation pathway is the sole aerobic route for phenylacetic acid metabolism in bacteria and facilitates degradation of environmental pollutants such as styrene and ethylbenzene. The phenylacetic acid pathway also is implicated in promoting Burkholderia cenocepacia infections in cystic fibrosis patients
physiological function
-
PCL is a side-chain precursor activation enzyme essentially involved in the pathway of penicillin biosynthesis, overview
-
physiological function
-
in a mutant lacking a 6-phophogluconate dehydratase and therefore unable to produce 2-keto-3-deoxy-6-phosphogluconate, phenylacetyl-CoA ligase activity is high, even in the presence of glucose plus phenylacetic acid. In wild-type, phenylacetyl-CoA ligase activity is low under these conditions
-
physiological function
-
isozyme PaaK1 does not play a distinct role in pathogenesis of Burkholderia cenocepacia in Caenorhabditis elegans, although the catabolic pathway for phenylacetic acid degradation is a requirement for full pathogenesis
-
physiological function
-
the phenylacetic acid degradation pathway is the sole aerobic route for phenylacetic acid metabolism in bacteria and facilitates degradation of environmental pollutants such as styrene and ethylbenzene. The PAA pathway also is implicated in promoting Burkholderia cenocepacia infections in cystic fibrosis patients
-
physiological function
-
the phenylacetic acid degradation pathway is the sole aerobic route for phenylacetic acid metabolism in bacteria and facilitates degradation of environmental pollutants such as styrene and ethylbenzene. The phenylacetic acid pathway also is implicated in promoting Burkholderia cenocepacia infections in cystic fibrosis patients
-
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conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental for antibiotic production
additional information
-
conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental for antibiotic production. The number of peroxisomes in a dnm1 overexpression strain variant is enhanced relative to those of wild-type controls
additional information
adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
additional information
adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
additional information
-
adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
additional information
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2
additional information
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2
additional information
-
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2
additional information
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2. The paaK1 deletion mutant IAI1 does not show any growth-defective phenotype in phenylacetate
additional information
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2. The paaK1 deletion mutant IAI1 does not show any growth-defective phenotype in phenylacetate
additional information
-
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2. The paaK1 deletion mutant IAI1 does not show any growth-defective phenotype in phenylacetate
additional information
isozyme PaaK1 shows dynamic enzyme-substrate interactions. Adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
additional information
isozyme PaaK1 shows dynamic enzyme-substrate interactions. Adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
additional information
-
isozyme PaaK1 shows dynamic enzyme-substrate interactions. Adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
additional information
-
conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental for antibiotic production
-
additional information
-
conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental for antibiotic production. The number of peroxisomes in a dnm1 overexpression strain variant is enhanced relative to those of wild-type controls
-
additional information
-
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2. The paaK1 deletion mutant IAI1 does not show any growth-defective phenotype in phenylacetate
-
additional information
-
isozyme PaaK1 shows dynamic enzyme-substrate interactions. Adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
-
additional information
-
insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2
-
additional information
-
adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview
-