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Literature summary for 1.14.14.9 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

Organism UniProt Comment Textmining
Acinetobacter baumannii Q6Q272 oxygenase component C2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminophenylacetate + FMNH2 + O2
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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

Synonyms Comment Organism
C2-hpah
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Acinetobacter baumannii

pH Range

pH Minimum pH Maximum Comment Organism
6
-
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
9
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substrate can bind to mutant S146A at both pH 6.0 and 9.0 Acinetobacter baumannii