Literature summary 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.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
1.14.14.9	4-hydroxyphenylacetate	-	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 + FMNH2 + O2	Acinetobacter baumannii	-	3,4-dihydroxyphenylacetate + FMN + H2O	-	?
1.14.14.9	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

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

Substrates and Products (Substrate)

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

EC Number	Synonyms	Comment	Organism
1.14.14.9	4-hydroxyphenylacetate 3-hydroxylase	-	Acinetobacter baumannii
1.14.14.9	HPA 3-hydroxylase	-	Acinetobacter baumannii
1.14.14.9	HPAH	-	Acinetobacter baumannii

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.14.14.9	FMN	-	Acinetobacter baumannii

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Release 2023.1 (January 2023)