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Literature summary for 1.14.14.9 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)

Cloned (Comment) Organism
-
Acinetobacter baumannii

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

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

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
FADH2
-
Acinetobacter baumannii