EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.192 | KCl | 110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration | Bos taurus | |
2.3.1.192 | phosphate | 37 mM, 140-175% of initial activity at low and high substrate concentration | Bos taurus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.71 | 3'-dephospho-CoA | - |
Bos taurus | |
2.3.1.71 | CoA | in absence of KCl, 0.1 mM CoA inhibits activity over 40% irrespective of the concentration of glycine. In presence of KCl, CoA inhibits activity only slightly, less than 10%. In presence of potassium phosphate the inhibition is reduced to less than 2%. 2.5 mM, almost complete inhibition of salt-free enzyme | Bos taurus | |
2.3.1.71 | hippuric acid | competitive with respect to benzoyl-CoA | Bos taurus | |
2.3.1.71 | K+ | K+ is a competitive inhibitor for benzoyl-coenzyme A, not a competitive inhibitor for salicylyl-CoA, K+ increases Km-value for glycine 10fold | Bos taurus | |
2.3.1.71 | Li+ | 110 mM | Bos taurus | |
2.3.1.71 | Mg2+ | - |
Bos taurus | |
2.3.1.71 | Na+ | 110 mM | Bos taurus | |
2.3.1.71 | potassium phosphate | - |
Bos taurus | |
2.3.1.71 | Rb+ | 110 mM | Bos taurus | |
2.3.1.192 | citrate | 40 mM, 22% residual activity | Bos taurus | |
2.3.1.192 | CoA | at physiologic concentrations of substrate, the arylacetyl transferase is extensively inhibited by CoA, inhibition is greatly reduced by ions. The 3-phosphate group on CoA is important for binding to the salt-free enzyme but in the presence of ions its importance is diminished | Bos taurus | |
2.3.1.192 | K2SO4 | 55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration | Bos taurus | |
2.3.1.192 | KCl | 110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration. Inhibition results in a large decrease in the affinity of the enzyme for phenylacetyl-CoA. In the presence of KCl the KD values for phenylacetyl-CoA and naphthylacetyl-CoA are similar, but the KD for glycine is extremely high for 1-naphthylacetyl-CoA conjugation | Bos taurus | |
2.3.1.192 | Mg2+ | 1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration | Bos taurus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.71 | 2 | - |
glycine | reaction with benzoyl-CoA or salicylyl-CoA | Bos taurus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.3.1.71 | mitochondrion | - |
Bos taurus | 5739 | - |
2.3.1.192 | mitochondrion | - |
Bos taurus | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.192 | Ca2+ | activation at both physiological and high substrate concentration | Bos taurus | |
2.3.1.192 | K2SO4 | 55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration | Bos taurus | |
2.3.1.192 | Mg2+ | 1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concentration | Bos taurus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.71 | 34000 | - |
gel filtration | Bos taurus |
2.3.1.192 | 32000 | - |
gel filtration | Bos taurus |
2.3.1.192 | 33500 | - |
1 * 33500, SDS-PAGE | Bos taurus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.71 | Bos taurus | - |
- |
- |
2.3.1.192 | Bos taurus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.71 | - |
Bos taurus |
2.3.1.192 | - |
Bos taurus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.3.1.71 | liver | - |
Bos taurus | - |
2.3.1.192 | liver | - |
Bos taurus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.1.71 | 1 | - |
- |
Bos taurus |
2.3.1.192 | 49 | - |
pH 8.0, 30°C | Bos taurus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.71 | benzoyl-CoA + glycine | - |
Bos taurus | CoA + N-benzoylglycine | - |
? | |
2.3.1.71 | salicyl-CoA + glycine | - |
Bos taurus | CoA + salicyluric acid | - |
? | |
2.3.1.192 | 1-naphthylacetyl-CoA + glycine | best substrate | Bos taurus | 1-naphthylacetylglycine + CoA | - |
? | |
2.3.1.192 | additional information | arginine and glutamine can substitute for glycine in the phenylacetyl-CoA assay and, while the rates are lower, they are equivalently affected by salt. No substrate: benzoyl-CoA, butyryl-CoA, and salicyl-CoA | Bos taurus | ? | - |
? | |
2.3.1.192 | phenylacetyl-CoA + glycine | best substrate | Bos taurus | phenylacetylglycine + CoA | - |
? | |
2.3.1.192 | phenylacetyl-CoA + L-arginine | at 20% of the rate with glycine | Bos taurus | ? + CoA | - |
? | |
2.3.1.192 | phenylacetyl-CoA + L-glutamine | at 6% of the rate with glycine | Bos taurus | ? + CoA | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.192 | monomer | 1 * 33500, SDS-PAGE | Bos taurus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.71 | 0.03 | - |
hippuric acid | - |
Bos taurus |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
2.3.1.192 | Bos taurus | isoelectric focusing | - |
7.5 |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.3.1.192 | 0.1 | - |
pH 8.0, 30°C, assay at 3.5 mM glycine, 0.020 mM phenylacetyl-CoA and in the absence of ions | Bos taurus | CoA |