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
-
phenylacetic
- penicillin
- chrysogenum
- putida
- ligases
- isopenicillin
- cenocepacia
- phenylglyoxylate
- benzoyl-coa
-
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
ECTree
6.2.1.30 phenylacetate-CoA ligaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 6.2.1.30 - phenylacetate-CoA ligase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + butyric acid + CoA
AMP + diphosphate + butyryl-CoA
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-
-
?
ATP + phenylacetate + CoA
?
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first enzyme involved in the aerobic catabolism of phenylacetic acid
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-
?
ATP + phenylacetate + CoA
?
-
the metabolism of phenylacetic acid starts by its activation to phenylacetyl-CoA via an aerobically induced phenylacetate-coenzyme A ligase
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-
?
ATP + phenylacetate + CoA
?
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enzyme is involved in the catabolism of phenylacetic acid
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-
?
ATP + phenylacetate + CoA
?
-
first enzyme involved in the aerobic catabolism of phenylacetic acid
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-
?
ATP + phenylacetate + CoA
?
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specifically induced by phenylacetic acid
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-
?
ATP + phenylacetate + CoA
?
-
first step in anaerobic degradation pathway of phenylacetate
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-
?
ATP + phenylacetate + CoA
?
-
first step in anaerobic degradation pathway of phenylacetate
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-
?
ATP + phenylacetate + CoA
?
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the enzyme is involved in anaerobic metabolism of L-phenylalanine via benzoyl-CoA
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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phenylacetate-CoA ligase is involved in penicillin production. The enzyme lacks a peptidyl carrier and behaves as an aryl-capping enzyme that activates phenylacetic acid and transfers it to the isopenicillin N acyltransferase. It is proposed that phenylacetate-CoA ligase and isopenicillin N-acyltransferase form a peroxisomal functional complex
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
PhlB might participate in the activation of phenylacetic acid during penicillin biosynthesis in Penicillium chrysogenum
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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the phenylacetyl-CoA ligase encoded by the phl gene is involved in penicillin production. The Phl protein lacks a peptide-carrier-protein domain and behaves as an aryl-capping enzyme that activates phenylacetic acid and transfers it to the isopenicillin N acyltransferase
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of phenylacetic acid and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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phenylacetate-CoA ligase is involved in penicillin production. The enzyme lacks a peptidyl carrier and behaves as an aryl-capping enzyme that activates phenylacetic acid and transfers it to the isopenicillin N acyltransferase. It is proposed that phenylacetate-CoA ligase and isopenicillin N-acyltransferase form a peroxisomal functional complex
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
the phenylacetyl-CoA ligase encoded by the phl gene is involved in penicillin production. The Phl protein lacks a peptide-carrier-protein domain and behaves as an aryl-capping enzyme that activates phenylacetic acid and transfers it to the isopenicillin N acyltransferase
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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the first step of this phenylacetate degradation pathway is catalysed by paaF-encoded phenylacetyl-CoA ligases that produce phenylacetyl-CoA
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
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the first step of this phenylacetate degradation pathway is catalysed by paaF-encoded phenylacetyl-CoA ligases that produce phenylacetyl-CoA
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism
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-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism
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-
?
additional information
?
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isozyme PaaK1 displays a lower Km for phenylacetic acid and broader substrate specificity than isozyme PaaK2
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-
?
additional information
?
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isozyme PaaK1 displays a lower Km for phenylacetic acid and broader substrate specificity than isozyme PaaK2
-
-
?
additional information
?
-
-
isozyme PaaK1 displays a lower Km for phenylacetic acid and broader substrate specificity than isozyme PaaK2
-
-
?
additional information
?
-
isozyme PaaK1 is more active than isozyme PaaK2, the larger binding pocket of PaaK1 can accommodate hydroxylated phenylacetate-derived molecules such as 3-hydroxyphenylacetic acid and 4-hydroxyphenylacetic acid, PaaK1 shows higher activity and broader substrate specificity than PaaK2
-
-
?
additional information
?
-
isozyme PaaK1 is more active than isozyme PaaK2, the larger binding pocket of PaaK1 can accommodate hydroxylated phenylacetate-derived molecules such as 3-hydroxyphenylacetic acid and 4-hydroxyphenylacetic acid, PaaK1 shows higher activity and broader substrate specificity than PaaK2
-
-
?
additional information
?
-
-
isozyme PaaK1 is more active than isozyme PaaK2, the larger binding pocket of PaaK1 can accommodate hydroxylated phenylacetate-derived molecules such as 3-hydroxyphenylacetic acid and 4-hydroxyphenylacetic acid, PaaK1 shows higher activity and broader substrate specificity than PaaK2
-
-
?
additional information
?
-
isozyme PaaK1 is more active than isozyme PaaK2, the larger binding pocket of PaaK1 can accommodate hydroxylated phenylacetate-derived molecules such as 3-hydroxyphenylacetic acid and 4-hydroxyphenylacetic acid, PaaK1 shows higher activity and broader substrate specificity than PaaK2
-
-
?
additional information
?
-
isozyme PaaK1 is more active than isozyme PaaK2, the larger binding pocket of PaaK1 can accommodate hydroxylated phenylacetate-derived molecules such as 3-hydroxyphenylacetic acid and 4-hydroxyphenylacetic acid, PaaK1 shows higher activity and broader substrate specificity than PaaK2
-
-
?
additional information
?
-
isozyme PaaK1 displays a lower Km for phenylacetic acid and broader substrate specificity than isozyme PaaK2
-
-
?
additional information
?
-
isozyme PaaK1 displays a lower Km for phenylacetic acid and broader substrate specificity than isozyme PaaK2
-
-
?
additional information
?
-
-
regulation of the paaF2 gene, the otherwise metabolically redundant PaaF2 auxiliary enzyme provides a system for rapid co-ordinate de-repression of the two sets of catabolic genes required for styrene degradation, overview. paaF2-encoded phenylacetate-CoA ligase activity is only induced in response to styrene in vivo and can be considered a styrene-specific phenylacetate-CoA ligase
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-
?
additional information
?
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-
regulation of the paaF2 gene, the otherwise metabolically redundant PaaF2 auxiliary enzyme provides a system for rapid co-ordinate de-repression of the two sets of catabolic genes required for styrene degradation, overview. paaF2-encoded phenylacetate-CoA ligase activity is only induced in response to styrene in vivo and can be considered a styrene-specific phenylacetate-CoA ligase
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-
?
