Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Protein Variants Comment Organism
1.14.14.9 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

EC Number Organism UniProt Comment Textmining
1.14.14.9 Acinetobacter baumannii Q6Q272 oxygenase component C2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.9 4-aminophenylacetate + FMNH2 + O2
-
 Acinetobacter baumannii 4-amino-3,5-dihydroxyphenylacetate + FMN + H2O
-
 ?
1.14.14.9 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

EC Number Synonyms Comment Organism
1.14.14.9 C2-hpah
-
 Acinetobacter baumannii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.14.14.9 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
1.14.14.9 9
-
 substrate can bind to mutant S146A at both pH 6.0 and 9.0 Acinetobacter baumannii