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Literature summary for 6.2.1.30 extracted from
- Phenylacetate metabolism in thermophiles: characterization of phenylacetate-CoA ligase, the initial enzyme of the hybrid pathway in Thermus thermophilus (2008), Curr. Microbiol., 57, 27-32.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzymatic activity is upregulated during growth on phenylacetate or phenylalanine | Thermus thermophilus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene paaK, DNA and amino acid sequence determination, expression of His6-tagged enzyme in Escherichia coli | Thermus thermophilus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.006 | - |
ATP | pH 7.8, 75°C, recombinant enzyme | Thermus thermophilus |  |
| 0.03 | - |
CoA | pH 7.8, 75°C, recombinant enzyme | Thermus thermophilus | |
| 0.05 | - |
phenylacetate | pH 7.8, 75°C, recombinant enzyme | Thermus thermophilus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | dependent on | Thermus thermophilus | |
| Mn2+ | can substitute for Mg2+ resulting in 90% of maximal activity | Thermus thermophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51000 | - |
2 * 51000, recombinant enzyme, SDS-PAGE | Thermus thermophilus |
| 110000 | - |
recombinant enzyme, gel filtration | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + phenylacetate + CoA | Thermus thermophilus | phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism | AMP + diphosphate + phenylacetyl-CoA | - |
? | |
| ATP + phenylacetate + CoA | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism | AMP + diphosphate + phenylacetyl-CoA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q72K16 | gene paaK | - |
| Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | Q72K16 | gene paaK | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli | Thermus thermophilus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture condition:L-phenylalanine-grown cell | - |
Thermus thermophilus | - |
| culture condition:phenylacetic acid-grown cell | - |
Thermus thermophilus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
no activity in acetate-grown cells | Thermus thermophilus |
| 0.001 | - |
below, glycerol-grown cells | Thermus thermophilus |
| 0.018 | - |
phenylacetate-grown cells | Thermus thermophilus |
| 0.025 | - |
phenylalanine-grown cells | Thermus thermophilus |
| 24 | - |
purified recombinant enzyme | Thermus thermophilus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, purified recombinant enzyme, 72 h no loss of activity, in the presence of 10% glycerol stable for up to 3 weeks | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 4-hydroxyphenylacetate + CoA | eightfold lower activity compared to phenylacetate | Thermus thermophilus | AMP + diphosphate + 4-hydroxyphenylacetyl-CoA | - |
? | |
| ATP + 4-hydroxyphenylacetate + CoA | eightfold lower activity compared to phenylacetate | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | AMP + diphosphate + 4-hydroxyphenylacetyl-CoA | - |
? | |
| ATP + phenylacetate + CoA | phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism | Thermus thermophilus | AMP + diphosphate + phenylacetyl-CoA | - |
? | |
| ATP + phenylacetate + CoA | i.e. PAA, highly specific for | Thermus thermophilus | AMP + diphosphate + phenylacetyl-CoA | - |
? | |
| ATP + phenylacetate + CoA | phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | AMP + diphosphate + phenylacetyl-CoA | - |
? | |
| ATP + phenylacetate + CoA | i.e. PAA, highly specific for | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | AMP + diphosphate + phenylacetyl-CoA | - |
? | |
| additional information | substrate specificity, no activity with other hydroxyl-substituted phenylacetic acids, monoaromatic acids, or nonaromatic acids, overview | Thermus thermophilus | ? | - |
? | |
| additional information | substrate specificity, no activity with other hydroxyl-substituted phenylacetic acids, monoaromatic acids, or nonaromatic acids, overview | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 51000, recombinant enzyme, SDS-PAGE | Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
- |
Thermus thermophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 90 | - |
Thermus thermophilus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 20 | - |
phenylacetate | pH 7.8, 75°C, recombinant enzyme | Thermus thermophilus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8 | - |
Thermus thermophilus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | - |
Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Thermus thermophilus | |
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