Literature summary for 1.17.9.1 extracted from

Efimov, I.; Cronin, C.N.; McIntire, W.S.
Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase (2001), Biochemistry, 40, 2155-2166.

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Protein Variants

Protein Variants	Comment	Organism
apo-PchF[Y384F]	the mutant Y384F of the flavoprotein subunit displays stoichiometric noncovalent FAD binding. The mutant flavoprotein subunit associates with the cytochrome subunit, although not as avidly as the wild-type flavoprotein subunit containing covalently bound FAD	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-cresol + acceptor + H2O	the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde	Pseudomonas putida	4-hydroxybenzaldehyde + reduced acceptor	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FAD	FAD is covalently attached to Tyr384. The mutant Y384F of the flavoprotein subunit displays stoichiometric noncovalent FAD binding	Pseudomonas putida

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Release 2023.1 (January 2023)