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Literature summary for extracted from

  • Dhammaraj, T.; Pinthong, C.; Visitsatthawong, S.; Tongsook, C.; Surawatanawong, P.; Chaiyen, P.
    A single-site mutation at Ser146 expands the reactivity of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase (2016), ACS Chem. Biol., 11, 2889-2896 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S146A mutation in oxygenase component C2, mutant is more effective than the wild-type in catalyzing the hydroxylation of 4-aminophenylacetate. Both variants first hydroxylate to give 3-hydroxy-4-aminophenylacetate, which is further hydroxylated to give 3,5-dihydroxy-4-aminophenylacetate Acinetobacter baumannii


Organism UniProt Comment Textmining
Acinetobacter baumannii Q6Q272 oxygenase component C2

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminophenylacetate + FMNH2 + O2
Acinetobacter baumannii 4-amino-3,5-dihydroxyphenylacetate + FMN + H2O
additional information wild-type shows a hydroxylation rate constant (kOH) for 4-aminophenylacetate of 0.028 per s compared to 17 per s for 4-hydroxyphenylacetate. Mutant S146A shows hydroxylation rate constants of 2.6 per s for 4-aminophenylacetate compared to 2.5 per s for 4-hydroxyphenylacetate Acinetobacter baumannii ?


Synonyms Comment Organism
Acinetobacter baumannii

pH Range

pH Minimum pH Maximum Comment Organism
substrate 4-aminophenylacetate can only bind to the wild-type enzyme at pH 6.0, substrate can bind to mutant S146A at both pH 6.0 and 9.0 Acinetobacter baumannii
substrate can bind to mutant S146A at both pH 6.0 and 9.0 Acinetobacter baumannii