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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.13.149 | expressed in Pseudomonas sp. strain Y2 | Escherichia coli |
2.3.1.16 | recombinant expression of tagged enzyme | Pseudomonas sp. |
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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | Pseudomonas sp. Y2 | - |
(3S)-3-hydroxyadipyl-CoA | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.35 | Escherichia coli | - |
- |
- |
1.1.1.35 | Pseudomonas sp. | - |
- |
- |
1.1.1.35 | Pseudomonas sp. Y2 | - |
- |
- |
1.2.1.91 | Escherichia coli | - |
- |
- |
1.14.13.149 | Escherichia coli | - |
- |
- |
2.3.1.16 | Pseudomonas sp. | - |
gene paaJ | - |
2.3.1.16 | Pseudomonas sp. Y2 | - |
gene paaJ | - |
2.3.1.223 | Pseudomonas sp. | Q845J8 | putative | - |
2.3.1.223 | Pseudomonas sp. Y2 | Q845J8 | putative | - |
3.3.2.12 | Escherichia coli | - |
- |
- |
4.2.1.17 | Escherichia coli | P76082 | gene paaF encoded in the paa gene cluster | - |
4.2.1.17 | Pseudomonas putida | - |
gene paaF encoded in the paa gene cluster | - |
4.2.1.17 | Pseudomonas sp. | - |
gene paaF encoded in the paa gene cluster | - |
4.2.1.17 | Pseudomonas sp. Y2 | - |
gene paaF encoded in the paa gene cluster | - |
5.3.3.18 | Pseudomonas sp. | - |
- |
- |
5.3.3.18 | Pseudomonas sp. Y2 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.91 | Ni2+-affinity column chromatography or amylose resin column chromatography | Escherichia coli |
1.14.13.149 | amylose resin column chromatography | Escherichia coli |
2.3.1.16 | recombinant tagged enzyme by affinity chromatography | Pseudomonas sp. |
3.3.2.12 | Ni2+-affinity column chromatography or amylose resin column chromatography | Escherichia coli |
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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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+ | - |
? | |
1.2.1.91 | 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O | - |
Escherichia coli | 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+ | - |
? | |
1.2.1.91 | additional information | the bifunctional enzyme also performs conversion of oxepin-CoA into 3-oxo-5,6-dehydrosuberyl-CoA | Escherichia coli | ? | - |
? | |
1.14.13.149 | phenylacetyl-CoA + O2 + NADPH + H+ | - |
Escherichia coli | 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+ | - |
ir | |
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 | - |
? | |
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 | - |
? | |
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 | ? | - |
? | |
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 | - |
? | |
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 | ? | - |
? | |
3.3.2.12 | oxepin-CoA + H2O | - |
Escherichia coli | 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde | - |
? | |
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 | |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.35 | 3-hydroxyadipyl-CoA dehydrogenase | - |
Escherichia coli |
1.1.1.35 | 3-hydroxyadipyl-CoA dehydrogenase | - |
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 | 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. |
1.1.1.35 | PaaH | - |
Escherichia coli |
1.1.1.35 | PaaH | - |
Pseudomonas sp. |
1.2.1.91 | oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) | bifunctional protein | Escherichia coli |
1.2.1.91 | paaZ | - |
Escherichia coli |
1.14.13.149 | PaaABCDE | - |
Escherichia coli |
1.14.13.149 | PaaAC(D) | - |
Escherichia coli |
2.3.1.16 | 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase | - |
Pseudomonas sp. |
2.3.1.16 | beta-ketothiolase | - |
Pseudomonas sp. |
2.3.1.16 | PaaJ | - |
Pseudomonas sp. |
3.3.2.12 | oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+) | bifunctional protein | Escherichia coli |
3.3.2.12 | paaZ | - |
Escherichia coli |
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 | 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 |
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. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.16 | 30 | - |
assay at | Pseudomonas sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.16 | 8 | - |
assay at | Pseudomonas sp. |
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 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.35 | physiological function | PaaH functions as an NAD+-dependent [probably (S)-3specific] 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)-3specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview | Pseudomonas sp. |
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. |
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 |