Literature summary for 1.14.13.244 extracted from

Cadieux, E.; Vrajmasu, V.; Achim, C.; Powlowski, J.; Muenck, E.
Biochemical, Moessbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600 (2002), Biochemistry, 41, 10680-10691 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	subunit DmpP is a [2Fe-2S]-containing reductase	Pseudomonas sp. CF600

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp. CF600	P19734 and P19731 and P19730 and P19732 and P19733	P19734 i.e FAD- and [2Fe-2S]-containing reductase DmpP, P19731 i.e. activator protein DmpM, P19730 i.e. oxygenase component DmpL, P19732 i.e. oxygenase component DmpN, P19733 i.e. oxygenase component DmpO	-

Cofactor

Cofactor	Comment	Organism	Structure
2Fe-2S-center	subunit DmpP is a [2Fe-2S]-containing reductase	Pseudomonas sp. CF600
FAD	-	Pseudomonas sp. CF600

General Information

General Information	Comment	Organism
physiological function	phenol hydroxylase comprises three components: DmpP is an FAD- and [2Fe-2S]-containing reductase, DmpM is a cofactorless activator protein, and DmpLNO is the oxygenase. DmpLNO contains the active site, but requires DmpM for efficient turnover. The steady-state turnover rate reaches a maximum at 1.5 DmpM:1 DmpLNO. DmpM interacts with the large subunit of the DmpLNO oxygenase complex. The active site of the oxygenase can accommodate two types of diiron clusters	Pseudomonas sp. CF600

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Release 2023.1 (January 2023)