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Literature summary extracted from

  • 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 (2008), Curr. Microbiol., 57, 27-32.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.2.1.30 additional information enzymatic activity is upregulated during growth on phenylacetate or phenylalanine Thermus thermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.30 gene paaK, DNA and amino acid sequence determination, expression of His6-tagged enzyme in Escherichia coli Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.30 0.006
-
 ATP pH 7.8, 75°C, recombinant enzyme Thermus thermophilus
6.2.1.30 0.03
-
 CoA pH 7.8, 75°C, recombinant enzyme Thermus thermophilus
6.2.1.30 0.05
-
 phenylacetate pH 7.8, 75°C, recombinant enzyme Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.30 Mg2+ dependent on Thermus thermophilus
6.2.1.30 Mn2+ can substitute for Mg2+ resulting in 90% of maximal activity Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.2.1.30 51000
-
 2 * 51000, recombinant enzyme, SDS-PAGE Thermus thermophilus
6.2.1.30 110000
-
 recombinant enzyme, gel filtration Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.30 ATP + phenylacetate + CoA Thermus thermophilus phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism AMP + diphosphate + phenylacetyl-CoA
-
 ?
6.2.1.30 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

EC Number Organism UniProt Comment Textmining
6.2.1.30 Thermus thermophilus Q72K16 gene paaK
-
6.2.1.30 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 Q72K16 gene paaK
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.30 recombinant His6-tagged enzyme from Escherichia coli Thermus thermophilus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.2.1.30 culture condition:L-phenylalanine-grown cell
-
 Thermus thermophilus
-
6.2.1.30 culture condition:phenylacetic acid-grown cell
-
 Thermus thermophilus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.2.1.30 additional information
-
 no activity in acetate-grown cells Thermus thermophilus
6.2.1.30 0.001
-
 below, glycerol-grown cells Thermus thermophilus
6.2.1.30 0.018
-
 phenylacetate-grown cells Thermus thermophilus
6.2.1.30 0.025
-
 phenylalanine-grown cells Thermus thermophilus
6.2.1.30 24
-
 purified recombinant enzyme Thermus thermophilus

Storage Stability

EC Number Storage Stability Organism
6.2.1.30 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.30 ATP + 4-hydroxyphenylacetate + CoA eightfold lower activity compared to phenylacetate Thermus thermophilus AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
-
 ?
6.2.1.30 ATP + 4-hydroxyphenylacetate + CoA eightfold lower activity compared to phenylacetate Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 AMP + diphosphate + 4-hydroxyphenylacetyl-CoA
-
 ?
6.2.1.30 ATP + phenylacetate + CoA phenylacetate-CoA ligase catalyzes the inital step of phenylacetate metabolism in the organism Thermus thermophilus AMP + diphosphate + phenylacetyl-CoA
-
 ?
6.2.1.30 ATP + phenylacetate + CoA i.e. PAA, highly specific for Thermus thermophilus AMP + diphosphate + phenylacetyl-CoA
-
 ?
6.2.1.30 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
-
 ?
6.2.1.30 ATP + phenylacetate + CoA i.e. PAA, highly specific for Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 AMP + diphosphate + phenylacetyl-CoA
-
 ?
6.2.1.30 additional information substrate specificity, no activity with other hydroxyl-substituted phenylacetic acids, monoaromatic acids, or nonaromatic acids, overview Thermus thermophilus ?
-
 ?
6.2.1.30 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

EC Number Subunits Comment Organism
6.2.1.30 dimer 2 * 51000, recombinant enzyme, SDS-PAGE Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.30 75
-
-
 Thermus thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.2.1.30 50 90
-
 Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2.1.30 20
-
 phenylacetate pH 7.8, 75°C, recombinant enzyme Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.30 7.5 8
-
 Thermus thermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.2.1.30 6 9
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.30 ATP dependent on Thermus thermophilus