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ADP + phenylacetate + CoA
?
-
28% of the activity with ATP
-
-
?
ATP + 3,4-methylenedioxycinnamic acid + CoA
AMP + diphosphate + 3,4-methylenedioxycinnamoyl-CoA
high activity
-
-
?
ATP + 3-chlorophenylacetate + CoA
AMP + diphosphate + 3-chlorophenylacetyl-CoA
ATP + 3-ethoxycinnamic acid + CoA
AMP + diphosphate + 3-ethoxy-cinnamoyl-CoA
high activity
-
-
?
ATP + 3-hydroxyphenylacetate + CoA
AMP + diphosphate + 3-hydroxyphenylacetyl-CoA
ATP + 3-methoxycinnamic acid + CoA
AMP + diphosphate + 3-methoxy-cinnamoyl-CoA
high activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaryl-CoA
reaction of EC 6.2.1.12
-
-
?
ATP + 4-hydroxyphenylacetate + CoA
AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
85% of the activity with phenylacetate
-
-
?
ATP + butanoate + CoA
AMP + diphosphate + butanoyl-CoA
-
19% of the activity with phenylacetate
-
-
?
ATP + butyric acid + CoA
AMP + diphosphate + butyryl-CoA
-
-
-
?
ATP + caprate + CoA
AMP + diphosphate + capryl-CoA
-
-
-
?
ATP + caproate + CoA
AMP + diphosphate + caproyl-CoA
best substrate
-
-
?
ATP + caproic acid + CoA
AMP + diphosphate + caproyl-CoA
-
-
-
?
ATP + caprylate + CoA
AMP + diphosphate + caprylyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
ATP + myristic acid + CoA
AMP + diphosphate + myristoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmityl-CoA
low activity, reaction of EC 6.2.1.3
-
-
?
ATP + phenoxyacetate + CoA
AMP + diphosphate + phenoxyacetyl-CoA
ATP + phenoxyacetic acid + CoA
AMP + phenoxyacetyl-CoA + diphosphate
-
-
-
-
?
ATP + phenoxyacetic acid + hydroxylamine
AMP + phenylacetoxyhydroxamate + diphosphate
-
-
-
?
ATP + phenylacetate + CoA
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
ATP + phenylacetic acid + hydroxylamine
AMP + phenylacetylhydroxamate + diphosphate
-
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
47% of the activity with phenylacetate
-
-
?
ATP + propionic acid + CoA
AMP + diphosphate + propionyl-CoA
low activity
-
-
?
ATP + stearate + CoA
AMP + diphosphate + stearyl-CoA
very low activity, reaction of EC 6.2.1.3
-
-
?
ATP + trans-4-coumaric acid + CoA
AMP + diphosphate + trans-4-coumaroyl-CoA
-
-
-
?
ATP + trans-cinnamic acid + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
1000fold higher activity compared to PAA
-
-
?
CTP + phenylacetate + CoA
CMP + diphosphate + phenylacetyl-CoA
-
2.8% of the activity with ATP
-
-
?
UTP + phenylacetate + CoA
UMP + diphosphate + phenylacetyl-CoA
-
2.5% of the activity with ATP
-
-
?
additional information
?
-
ATP + 3-chlorophenylacetate + CoA
AMP + diphosphate + 3-chlorophenylacetyl-CoA
-
-
-
?
ATP + 3-chlorophenylacetate + CoA
AMP + diphosphate + 3-chlorophenylacetyl-CoA
-
-
-
?
ATP + 3-hydroxyphenylacetate + CoA
AMP + diphosphate + 3-hydroxyphenylacetyl-CoA
-
-
-
?
ATP + 3-hydroxyphenylacetate + CoA
AMP + diphosphate + 3-hydroxyphenylacetyl-CoA
-
-
-
?
ATP + 4-hydroxyphenylacetate + CoA
AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
-
-
-
?
ATP + 4-hydroxyphenylacetate + CoA
AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
-
-
-
?
ATP + 4-hydroxyphenylacetate + CoA
AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
eightfold lower activity compared to phenylacetate
-
-
?
ATP + 4-hydroxyphenylacetate + CoA
AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
eightfold lower activity compared to phenylacetate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
reaction of EC 6.2.1.12
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
reaction of EC 6.2.1.12
-
-
?
ATP + phenoxyacetate + CoA
AMP + diphosphate + phenoxyacetyl-CoA
low activity
-
-
?
ATP + phenoxyacetate + CoA
AMP + diphosphate + phenoxyacetyl-CoA
low activity
-
-
?
ATP + phenoxyacetate + CoA
AMP + diphosphate + phenoxyacetyl-CoA
low activity
-
-
?
ATP + phenylacetate + CoA
?
-
first enzyme involved in the aerobic catabolism of phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
the metabolism of phenylacetic acid starts by its activation to phenylacetyl-CoA via an aerobically induced phenylacetate-coenzyme A ligase
-
-
?
ATP + phenylacetate + CoA
?
-
enzyme is involved in the catabolism of phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
first enzyme involved in the aerobic catabolism of phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
specifically induced by phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
first step in anaerobic degradation pathway of phenylacetate
-
-
?
ATP + phenylacetate + CoA
?
-
first step in anaerobic degradation pathway of phenylacetate
-
-
?
ATP + phenylacetate + CoA
?
-
the enzyme is involved in anaerobic metabolism of L-phenylalanine via benzoyl-CoA
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
low activity
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
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
PhlB might participate in the activation of phenylacetic acid during penicillin biosynthesis in Penicillium chrysogenum
-
-
?
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
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
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
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
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
low activity
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
highly specific
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
the first step of this phenylacetate degradation pathway is catalysed by paaF-encoded phenylacetyl-CoA ligases that produce phenylacetyl-CoA
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
highly specific
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
the first step of this phenylacetate degradation pathway is catalysed by paaF-encoded phenylacetyl-CoA ligases that produce phenylacetyl-CoA
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
i.e. PAA, highly specific for
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
i.e. PAA, highly specific for
-
-
?
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
?
-
-
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
?
-
no activity 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
no activity 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
-
no activity 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
no activity with 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
no activity with 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
-
no activity with 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
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
?
-
no activity with 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
no activity with 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
no activity 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
no activity 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and 2-chloro-2-hydroxy-phenylacetate
-
-
?
additional information
?
-
-
only beta-substitued acetic acid can serve as substrate, not phenylpropionic acid
-
-
?
additional information
?
-
the enzyme also belongs to EC 6.2.1.2, substrate specificity of PCL, the more substituted compounds ferulic acid, caffeic acid and sinapic acid, which are substrates for most 4-coumarate CoA ligases, are very poor substrates for PCL. With the exception of acetic acid, all short and medium chain fatty acids tested are converted by PCL, PCL is able to activate all the side chains of these naturally occurring lactam side products, overview. Residues H265, I266, Y267, V270, F307, F335, G337, A338, G361, T369, V370, and K557 are involved in substrate binding
-
-
?
additional information
?
-
-
the enzyme also belongs to EC 6.2.1.2, substrate specificity of PCL, the more substituted compounds ferulic acid, caffeic acid and sinapic acid, which are substrates for most 4-coumarate CoA ligases, are very poor substrates for PCL. With the exception of acetic acid, all short and medium chain fatty acids tested are converted by PCL, PCL is able to activate all the side chains of these naturally occurring lactam side products, overview. Residues H265, I266, Y267, V270, F307, F335, G337, A338, G361, T369, V370, and K557 are involved in substrate binding
-
-
?
additional information
?
-
the enzyme displays broad substrate spectrum and shows higher activities to medium and long-chain fatty acids. The enzyme is also active with cinnamic acid and coumaric acid, see for EC 6.2.1.12
-
-
?
additional information
?
-
the enzyme displays broad substrate spectrum and shows higher activities to medium and long-chain fatty acids. The enzyme is also active with cinnamic acid and coumaric acid, see for EC 6.2.1.12
-
-
?
additional information
?
-
-
no activity with: 3-hydroxyphenylacetic acid, 4-hydroxyphenylacetic acid, 3,4-dihydroxyphenylacetic acid
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
substrate specificity, no activity with other hydroxyl-substituted phenylacetic acids, monoaromatic acids, or nonaromatic acids, overview
-
-
?
additional information
?
-
-
substrate specificity, no activity with other hydroxyl-substituted phenylacetic acids, monoaromatic acids, or nonaromatic acids, overview
-
-
?
additional information
?
-
substrate specificity, no activity with other hydroxyl-substituted phenylacetic acids, monoaromatic acids, or nonaromatic acids, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + butyric acid + CoA
AMP + diphosphate + butyryl-CoA
-
-
-
?
ATP + phenylacetate + CoA
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
additional information
?
-
ATP + phenylacetate + CoA
?
-
first enzyme involved in the aerobic catabolism of phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
the metabolism of phenylacetic acid starts by its activation to phenylacetyl-CoA via an aerobically induced phenylacetate-coenzyme A ligase
-
-
?
ATP + phenylacetate + CoA
?
-
enzyme is involved in the catabolism of phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
first enzyme involved in the aerobic catabolism of phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
specifically induced by phenylacetic acid
-
-
?
ATP + phenylacetate + CoA
?
-
first step in anaerobic degradation pathway of phenylacetate
-
-
?
ATP + phenylacetate + CoA
?
-
first step in anaerobic degradation pathway of phenylacetate
-
-
?
ATP + phenylacetate + CoA
?
-
the enzyme is involved in anaerobic metabolism of L-phenylalanine via benzoyl-CoA
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
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
PhlB might participate in the activation of phenylacetic acid during penicillin biosynthesis in Penicillium chrysogenum
-
-
?
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
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
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
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
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
the first step of this phenylacetate degradation pathway is catalysed by paaF-encoded phenylacetyl-CoA ligases that produce phenylacetyl-CoA
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
-
the first step of this phenylacetate degradation pathway is catalysed by paaF-encoded phenylacetyl-CoA ligases that produce phenylacetyl-CoA
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism
-
-
?
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
?
-
-
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
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additional information
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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
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additional information
?
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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
-
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additional information
?
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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
-
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?
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
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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
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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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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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evolution
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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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
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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physiological function
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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
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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
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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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additional information
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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
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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
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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
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Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
Anaerobic metabolism of L-phenylalanine via benzoyl-CoA in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
168
310-320
1997
Thauera aromatica
brenda
Martinez-Blanco, H.; Reglero, A.; Rodriguez-Aparicio, L.B.; Luengo, J.M.
Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida
J. Biol. Chem.
265
7084-7090
1990
Pseudomonas putida
brenda
Rodriguez-Aparacio, L.B.; Reglero, A.; Martinez-Blanco, H.; Luengo, J.M.
Fluorometric determination of phenylacetyl-CoA ligase from Pseudomonas putida: a very sensitive assay for a newly described enzyme
Biochim. Biophys. Acta
1073
431-433
1991
Pseudomonas putida
brenda
El-Said Mohamed, M.; Fuchs, G.
Purification and characterization of phenylacetyl-coenzyme A ligase from a denitrifying Pseudomonas sp., an enzyme involved in the anaerobic degradation of phenylacetate
Arch. Microbiol.
159
544-562 (c)
1993
Pseudomonas sp., Pseudomonas sp. KB 740
brenda
Kogekar, R.G.; Desphpande, V.N.
Biosynthesis of Penicillin in vitro: purification & properties of phenyl/phenoxyacetic acid activating enzyme
Indian J. Biochem. Biophys.
19
257-261
1982
Penicillium chrysogenum
brenda
Vitovski, S.
Phenylacetate-coenzyme A ligase is induced during growth on phenylacetic acid in different bacteria of several genera
FEMS Microbiol. Lett.
108
1-5
1993
Achromobacter denitrificans, Acinetobacter calcoaceticus, Acinetobacter calcoaceticus EGB, Burkholderia cepacia, Burkholderia cepacia 104P, Burkholderia cepacia 132P, Burkholderia cepacia 91P, Escherichia coli, Escherichia coli ATCC 11105, Providencia rettgeri, Providencia rettgeri ATCC 31052, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas putida 63P, Pseudomonas sp., Pseudomonas sp. MT14
brenda
Mohamed Mel, S.; Ismail, W.; Heider, J.; Fuchs, G.
Aerobic metabolism of phenylacetic acids in Azoarcus evansii
Arch. Microbiol.
178
180-192
2002
Aromatoleum evansii
brenda
Minambres, B.; Martinez-Blanco, H.; Olivera, E.R.; Garcia, B.; Diez, B.; Barredo, J.L.; Moreno, M.A.; Schleissner, C.; Salto, F.; Luengo, J.M.
Molecular cloning and expression in different microbes of the DNA encoding Pseudomonas putida U phenylacetyl-CoA ligase. Use of this gene to improve the rate of benzylpenicillin biosynthesis in Penicillium chrysogenum
J. Biol. Chem.
271
33531-33538
1996
Pseudomonas putida
brenda
Mohamed, M.E.S.
Biochemical and molecular characterization of phenylacetate-coenzyme A ligase, an enzyme catalyzing the first step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
J. Bacteriol.
182
286-294
2000
Aromatoleum evansii
brenda
Lamas-Maceiras, M.; Vaca, I.; Rodriguez, E.; Casqueiro, J.; Martin, J.F.
Amplification and disruption of the phenylacetyl-CoA ligase gene of Penicillium chrysogenum encoding an aryl-capping enzyme that supplies phenylacetic acid to the isopenicillin N acyltransferase
Biochem. J.
395
147-155
2005
Penicillium chrysogenum, Penicillium chrysogenum AS-P-78
brenda
Ward, P.G.; KE, O.C.
Induction and quantification of phenylacyl-CoA ligase enzyme activities in Pseudomonas putida CA-3 grown on aromatic carboxylic acids
FEMS Microbiol. Lett.
251
227-232
2005
Pseudomonas putida, Pseudomonas putida CA-3
brenda
Di Gennaro, P.; Ferrara, S.; Ronco, I.; Galli, E.; Sello, G.; Papacchini, M.; Bestetti, G.
Styrene lower catabolic pathway in Pseudomonas fluorescens ST: identification and characterization of genes for phenylacetic acid degradation
Arch. Microbiol.
188
117-125
2007
Pseudomonas fluorescens, Pseudomonas fluorescens ST
brenda
Wang, F.Q.; Liu, J.; Dai, M.; Ren, Z.H.; Su, C.Y.; He, J.G.
Molecular cloning and functional identification of a novel phenylacetyl-CoA ligase gene from Penicillium chrysogenum
Biochem. Biophys. Res. Commun.
360
453-458
2007
Penicillium chrysogenum (A7KUK6), Penicillium chrysogenum
brenda
Koetsier, M.J.; Jekel, P.A.; van den Berg, M.A.; Bovenberg, R.A.; Janssen, D.B.
Characterization of a phenylacetate-CoA ligase from Penicillium chrysogenum
Biochem. J.
417
467-476
2008
Penicillium chrysogenum (O74725), Penicillium chrysogenum
brenda
Erb, T.J.; Ismail, W.; Fuchs, G.
Phenylacetate metabolism in thermophiles: characterization of phenylacetate-CoA ligase, the initial enzyme of the hybrid pathway in Thermus thermophilus
Curr. Microbiol.
57
27-32
2008
Thermus thermophilus (Q72K16), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72K16)
brenda
del Peso-Santos, T.; Shingler, V.; Perera, J.
The styrene-responsive StyS/StyR regulation system controls expression of an auxiliary phenylacetyl-coenzyme A ligase: implications for rapid metabolic coupling of the styrene upper- and lower-degradative pathways
Mol. Microbiol.
69
317-330
2008
Pseudomonas sp., Pseudomonas sp. Y2
brenda
Kiel, J.A.; van den Berg, M.A.; Fusetti, F.; Poolman, B.; Bovenberg, R.A.; Veenhuis, M.; van der Klei, I.J.
Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells
Funct. Integr. Genomics
9
167-184
2009
Penicillium chrysogenum
brenda
Kim, J.; Yeom, J.; Jeon, C.O.; Park, W.
Intracellular 2-keto-3-deoxy-6-phosphogluconate is the signal for carbon catabolite repression of phenylacetic acid metabolism in Pseudomonas putida KT2440
Microbiology
155
2420-2428
2009
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Gidijala, L.; Kiel, J.A.; Douma, R.D.; Seifar, R.M.; van Gulik, W.M.; Bovenberg, R.A.; Veenhuis, M.; van der Klei, I.J.
An engineered yeast efficiently secreting penicillin
PLoS ONE
4
e8317
2009
Penicillium chrysogenum
brenda
Meijer, W.H.; Gidijala, L.; Fekken, S.; Kiel, J.A.; van den Berg, M.A.; Lascaris, R.; Bovenberg, R.A.; van der Klei, I.J.
Peroxisomes are required for efficient penicillin biosynthesis in Penicillium chrysogenum
Appl. Environ. Microbiol.
76
5702-5709
2010
Penicillium chrysogenum, Penicillium chrysogenum NRRL1951
brenda
Martin, J.F.; Ullan, R.V.; Garcia-Estrada, C.
Regulation and compartmentalization of beta-lactam biosynthesis
Microb. Biotechnol.
3
285-299
2010
Penicillium sp.
brenda
Yu, Z.L.; Liu, J.; Wang, F.Q.; Dai, M.; Zhao, B.H.; He, J.G.; Zhang, H.
Cloning and characterization of a novel CoA-ligase gene from Penicillium chrysogenum
Folia Microbiol. (Praha)
56
246-252
2011
Penicillium chrysogenum (D3GE78), Penicillium chrysogenum WIS 54-1255 (D3GE78)
brenda
Imolorhe, I.A.; Cardona, S.T.
3-Hydroxyphenylacetic acid induces the Burkholderia cenocepacia phenylacetic acid degradation pathway - toward understanding the contribution of aromatic catabolism to pathogenesis
Front. Cell. Infect. Microbiol.
1
14
2011
Burkholderia cenocepacia (B4E7B5), Burkholderia cenocepacia (B4EL89), Burkholderia cenocepacia, Burkholderia cenocepacia DSM 16553 (B4E7B5), Burkholderia cenocepacia DSM 16553 (B4EL89)
brenda
Law, A.; Boulanger, M.J.
Defining a structural and kinetic rationale for paralogous copies of phenylacetate-CoA ligases from the cystic fibrosis pathogen Burkholderia cenocepacia J2315
J. Biol. Chem.
286
15577-15585
2011
Burkholderia cenocepacia (B4E7B5), Burkholderia cenocepacia (B4EL89), Burkholderia cenocepacia, Burkholderia cenocepacia DSM 16553 (B4E7B5), Burkholderia cenocepacia DSM 16553 (B4EL89)
brenda