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Literature summary for 1.14.14.9 extracted from

  • Phongsak, T.; Sucharitakul, J.; Thotsaporn, K.; Oonanant, W.; Yuvaniyama, J.; Svasti, J.; Ballou, D.P.; Chaiyen, P.
    The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain (2012), J. Biol. Chem., 287, 26213-26222.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
4-hydroxyphenylacetate
-
Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylacetate + FMNH2 + O2 Acinetobacter baumannii
-
3,4-dihydroxyphenylacetate + FMN + H2O
-
?
additional information Acinetobacter baumannii the enzyme utilizes the C-terminal domain of the reductase component as an autoinhibitory domain to suppress both the rate of reduction of FMN and the rate of release of FMNH2 from the reductase component ?
-
?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + FMNH2 + O2
-
Acinetobacter baumannii 3,4-dihydroxyphenylacetate + FMN + H2O
-
?
additional information the enzyme utilizes the C-terminal domain of the reductase component as an autoinhibitory domain to suppress both the rate of reduction of FMN and the rate of release of FMNH2 from the reductase component Acinetobacter baumannii ?
-
?

Synonyms

Synonyms Comment Organism
4-hydroxyphenylacetate 3-hydroxylase
-
Acinetobacter baumannii
HPA 3-hydroxylase
-
Acinetobacter baumannii
HPAH
-
Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
FMN
-
Acinetobacter baumannii