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Literature summary extracted from

  • Oonanant, W.; Sucharitakul, J.; Chaiyen, P.; Yuvaniyama, J.
    Crystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii (2012), Acta Crystallogr. Sect. F, 68, 720-723.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.9
-
 Acinetobacter baumannii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.9 microbatch method, using 20% (W/v) PEG 400, 0.1 M sodium acetate pH 4.6 as a precipitant Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.9 4-hydroxyphenylacetate + FADH2 + O2 Acinetobacter baumannii
-
 3,4-dihydroxyphenylacetate + FAD + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.9 Acinetobacter baumannii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.9 ammonium sulfate precipitation, DEAE-Sepharose column chromatography, phenyl Sepharose column chromatography, and G-25 gel filtration Acinetobacter baumannii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.9 4-hydroxyphenylacetate + FADH2 + O2
-
 Acinetobacter baumannii 3,4-dihydroxyphenylacetate + FAD + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.9 HPAH the protein comprises a smaller reductase and a larger oxygenase on separate polypeptide chains Acinetobacter baumannii
1.14.14.9 p-hydroxyphenylacetate 3-hydroxylase
-
 Acinetobacter baumannii

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.9 FADH2
-
 Acinetobacter baumannii