Literature summary extracted from

Palfey, B.A.; Entsch, B.; Ballou, D.P.; Massey, V.
Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp (1994), Biochemistry, 33, 1545-1554.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.14.13.2	N300D	330fold reduced reduction rate of the flavin of the enzyme by NADPH compared to wild-type enzyme, redox potential of the flavin is 20-40mV lower than that of the wild-type enzyme. The mutation interferes with the orientation of pyridine nucleotide and flavin during reduction, stabilizes flavin C(4a) intermediates, prevents substrate ionization, and alters the rates and strengths of ligand binding	Pseudomonas aeruginosa

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.13.2	Pseudomonas aeruginosa	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)