Literature summary for 1.14.13.244 extracted from

Powlowski, J.; Shingler, V.
In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600 (1990), J. Bacteriol., 172, 6834-6840 .

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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	-

Purification (Commentary)

Purification (Comment)	Organism
purification of subunit DmpP	Pseudomonas sp. CF600

Cofactor

Cofactor	Comment	Organism	Structure
2Fe-2S-center	subunit DmpP is a flavin adenine dinucleotide containing iron-sulfur protein	Pseudomonas sp. CF600
FAD	subunit PmpP	Pseudomonas sp. CF600

General Information

General Information	Comment	Organism
physiological function	subunit DmpP is a flavin adenine dinucleotide containing iron-sulfur protein and probably functions to transfer electrons from NAD(P)H to the iron-requiring oxygenase component	Pseudomonas sp. CF600

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Release 2023.1 (January 2023)