Literature summary extracted from

  • Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
    Bacterial phenylalanine and phenylacetate catabolic pathway revealed (2010), Proc. Natl. Acad. Sci. USA, 107, 14390-14395.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.149 additional information maltose-binding protein-tagged PaaD added separately does not affect the specific activity of PaaABCE significantly Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.16 recombinant expression of tagged enzyme Pseudomonas sp.
1.14.13.149 expressed in Pseudomonas sp. strain Y2 Escherichia coli

General Stability

EC Number General Stability Organism
1.14.13.149 the ability of PaaABC(D)E to oxygenate its substrate is largely lost within 5 min in an enzymatic assay (50 mMTris-HCl (pH 8.0) at 30°C) Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.17 2,3-didehydroadipyl-CoA + H2O Pseudomonas sp.
-
(3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O Pseudomonas putida
-
(3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O Escherichia coli
-
(3S)-3-hydroxyadipyl-CoA
-
r
1.1.1.35 (3S)-3-hydroxyadipyl-CoA + NAD+ Escherichia coli
-
3-oxoadipyl-CoA + NADH + H+
-
?
1.1.1.35 (3S)-3-hydroxyadipyl-CoA + NAD+ Pseudomonas sp.
-
3-oxoadipyl-CoA + NADH + H+
-
?
4.2.1.17 2,3-didehydroadipyl-CoA + H2O Pseudomonas sp. Y2
-
(3S)-3-hydroxyadipyl-CoA
-
r
1.1.1.35 (3S)-3-hydroxyadipyl-CoA + NAD+ Pseudomonas sp. Y2
-
3-oxoadipyl-CoA + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.35 Escherichia coli
-
-
-
1.2.1.91 Escherichia coli
-
-
-
3.3.2.12 Escherichia coli
-
-
-
1.14.13.149 Escherichia coli
-
-
-
4.2.1.17 Pseudomonas sp.
-
gene paaF encoded in the paa gene cluster
-
1.1.1.35 Pseudomonas sp.
-
-
-
2.3.1.16 Pseudomonas sp.
-
gene paaJ
-
5.3.3.18 Pseudomonas sp.
-
-
-
4.2.1.17 Pseudomonas putida
-
gene paaF encoded in the paa gene cluster
-
4.2.1.17 Escherichia coli P76082 gene paaF encoded in the paa gene cluster
-
2.3.1.223 Pseudomonas sp. Q845J8 putative
-
4.2.1.17 Pseudomonas sp. Y2
-
gene paaF encoded in the paa gene cluster
-
1.1.1.35 Pseudomonas sp. Y2
-
-
-
2.3.1.16 Pseudomonas sp. Y2
-
gene paaJ
-
5.3.3.18 Pseudomonas sp. Y2
-
-
-
2.3.1.223 Pseudomonas sp. Y2 Q845J8 putative
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.16 recombinant tagged enzyme by affinity chromatography Pseudomonas sp.
1.2.1.91 Ni2+-affinity column chromatography or amylose resin column chromatography Escherichia coli
3.3.2.12 Ni2+-affinity column chromatography or amylose resin column chromatography Escherichia coli
1.14.13.149 amylose resin column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.3.2.12 0.02
-
pH not specified in the publication, temperature not specified in the publication Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.91 additional information the bifunctional enzyme also performs conversion of oxepin-CoA into 3-oxo-5,6-dehydrosuberyl-CoA Escherichia coli ?
-
?
3.3.2.12 additional information the bifunctional protein also use 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and NADP+ as substrate yielding 3-oxo-5,6-dehydrosuberyl-CoA as main product Escherichia coli ?
-
?
2.3.1.223 additional information enzyme additionally catalyzes the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA, reaction of EC 2.3.1.174 Pseudomonas sp. ?
-
?
2.3.1.223 additional information enzyme additionally catalyzes the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA, reaction of EC 2.3.1.174 Pseudomonas sp. Y2 ?
-
?
1.2.1.91 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O
-
Escherichia coli 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+
-
?
3.3.2.12 oxepin-CoA + H2O
-
Escherichia coli 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
-
?
1.1.1.35 (3S)-3-hydroxyadipyl-CoA + NAD+
-
Escherichia coli 3-oxoadipyl-CoA + NADH + H+
-
?
1.1.1.35 (3S)-3-hydroxyadipyl-CoA + NAD+
-
Pseudomonas sp. 3-oxoadipyl-CoA + NADH + H+
-
?
1.1.1.35 (3S)-3-hydroxyadipyl-CoA + NAD+
-
Pseudomonas sp. Y2 3-oxoadipyl-CoA + NADH + H+
-
?
4.2.1.17 2,3-didehydroadipyl-CoA + H2O
-
Pseudomonas sp. (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O
-
Pseudomonas putida (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O
-
Escherichia coli (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O substrate and product identification by mass spectrometry Pseudomonas sp. (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O substrate and product identification by mass spectrometry Pseudomonas putida (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O substrate and product identification by mass spectrometry Escherichia coli (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O
-
Pseudomonas sp. Y2 (3S)-3-hydroxyadipyl-CoA
-
r
4.2.1.17 2,3-didehydroadipyl-CoA + H2O substrate and product identification by mass spectrometry Pseudomonas sp. Y2 (3S)-3-hydroxyadipyl-CoA
-
r
2.3.1.16 3-oxo-5,6-dehydrosuberyl-CoA + CoA
-
Pseudomonas sp. 2,3-dehydroadipyl-CoA + acetyl-CoA
-
?
2.3.1.16 3-oxo-5,6-dehydrosuberyl-CoA + CoA
-
Pseudomonas sp. Y2 2,3-dehydroadipyl-CoA + acetyl-CoA
-
?
1.14.13.149 phenylacetyl-CoA + O2 + NADPH + H+
-
Escherichia coli 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
-
ir
5.3.3.18 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin Pseudomonas sp. 2-oxepin-2(3H)-ylideneacetyl-CoA
-
?
5.3.3.18 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin Pseudomonas sp. Y2 2-oxepin-2(3H)-ylideneacetyl-CoA
-
?
3.3.2.12 2-oxepin-2(3H)-ylideneacetyl-CoA + H2O addition of purified PaaZ enzyme to enzymatically produced epoxide and oxepin in the presence of PaaG protein leads to a complete NADP+-dependent conversion of epoxide and oxepin into 3-oxo-5,6-dehydrosuberyl-CoA. PaaZ functions as an oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase catalyzing the two-step conversion of the oxepin-CoA via the open-chain aldehyde intermediate to 3-oxo-5,6-dehydrosuberyl-CoA Escherichia coli 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
-
?
2.3.1.223 CoA + 3-oxo-5,6-didehydrosuberoyl-CoA transforms the beta-keto C8 intermediate of phenylacetate catabolic pathway with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA Pseudomonas sp. 2,3-didehydroadipoyl-CoA + acetyl-CoA
-
?
2.3.1.223 CoA + 3-oxo-5,6-didehydrosuberoyl-CoA transforms the beta-keto C8 intermediate of phenylacetate catabolic pathway with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA Pseudomonas sp. Y2 2,3-didehydroadipoyl-CoA + acetyl-CoA
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.17 More PaaF is a member of the crotonase superfamily Pseudomonas sp.
4.2.1.17 More PaaF is a member of the crotonase superfamily Pseudomonas putida
4.2.1.17 More PaaF is a member of the crotonase superfamily Escherichia coli
1.1.1.35 More PaaH is a member of the alcohol dehydrogenase family Escherichia coli
1.1.1.35 More PaaH is a member of the alcohol dehydrogenase family Pseudomonas sp.
2.3.1.16 beta-ketothiolase
-
Pseudomonas sp.
1.2.1.91 paaZ
-
Escherichia coli
3.3.2.12 paaZ
-
Escherichia coli
1.2.1.91 oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) bifunctional protein Escherichia coli
3.3.2.12 oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) bifunctional protein Escherichia coli
1.14.13.149 PaaAC(D)
-
Escherichia coli
1.14.13.149 PaaABCDE
-
Escherichia coli
1.1.1.35 PaaH
-
Escherichia coli
1.1.1.35 PaaH
-
Pseudomonas sp.
1.1.1.35 3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific)
-
Escherichia coli
1.1.1.35 3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific)
-
Pseudomonas sp.
1.1.1.35 3-hydroxyadipyl-CoA dehydrogenase
-
Escherichia coli
1.1.1.35 3-hydroxyadipyl-CoA dehydrogenase
-
Pseudomonas sp.
2.3.1.16 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
-
Pseudomonas sp.
2.3.1.16 PaaJ
-
Pseudomonas sp.
4.2.1.17 2,3-dehydroadipyl-CoA hydratase
-
Pseudomonas sp.
4.2.1.17 2,3-dehydroadipyl-CoA hydratase
-
Pseudomonas putida
4.2.1.17 2,3-dehydroadipyl-CoA hydratase
-
Escherichia coli
4.2.1.17 PaaF
-
Pseudomonas sp.
4.2.1.17 PaaF
-
Pseudomonas putida
4.2.1.17 PaaF
-
Escherichia coli
5.3.3.18 paaG
-
Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.16 30
-
assay at Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.16 8
-
assay at Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.35 NAD+ specific for Escherichia coli
1.1.1.35 NAD+ specific for Pseudomonas sp.
1.14.13.149 NADPH
-
Escherichia coli

General Information

EC Number General Information Comment Organism
1.1.1.35 physiological function PaaH functions as an NAD+-dependent [probably (S)-3–specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview Escherichia coli
1.1.1.35 physiological function PaaH functions as an NAD+-dependent [probably (S)-3–specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview Pseudomonas sp.
3.3.2.12 physiological function enzyme is part of the catabolic pathway of phenylacetate. Intermediates are processed as CoA thioesters, and the aromatic ring of phenylacetyl-CoA becomes activated to a ring 1,2-epoxide by a distinct multicomponent oxygenase. The reactive nonaromatic epoxide is isomerized to a seven-member O-heterocyclic enol ether, an oxepin. This isomerization is followed by hydrolytic ring cleavage and beta-oxidation steps, leading to acetyl-CoA and succinyl-CoA Escherichia coli
4.2.1.17 metabolism the enzyme catalyzes a reaction step of the beta-oxidation, as part of the catabolic gene cluster for phenylacetate degradation, overview Escherichia coli
4.2.1.17 metabolism the enzyme catalyzes a reaction step of the beta-oxidation, overview Pseudomonas sp.
4.2.1.17 metabolism the enzyme catalyzes a reaction step of the beta-oxidation, overview Pseudomonas putida
2.3.1.16 metabolism the enzyme PaaJ is involved in the aerobic phenylacetate catabolic pathway. PaaJ, a beta-ketothiolase, transforms the resulting beta-keto C8 intermediate with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA, besides catalyzing the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA Pseudomonas sp.