Literature summary for 1.14.13.2 extracted from

Ortiz-Maldonado, M.; Aeschliman, S.M.; Ballou, D.P.; Masey, V.
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl flavin (2001), Biochemistry, 40, 8705-8716.

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Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzymes K297M, N300D and Y385F	Pseudomonas aeruginosa

Protein Variants

Protein Variants	Comment	Organism
K297M	decreased positive charge in active site, about 35fold slower hydroxylation rate than the wild-type enzyme. Substitution of 8-Cl-FAD in the mutant gives about 1.8fold increase in hydroxylation rate compared to the wild-type enzyme	Pseudomonas aeruginosa
N300D	decreased positive charge in active site, about 35fold slower hydroxylation rate than the wild-type enzyme, Substitution of 8-Cl-FAD in the mutant gives about 1.8fold increase in hydroxylation rate compared to the wild-type enzyme	Pseudomonas aeruginosa
Y385F	mutant enzyme with a disrupted hydrogen-bonding network, substitution of 8-Cl-FAD in the mutant gives about 1.5fold increase in hydroxylation rate compared to the wild-type enzyme	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

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Release 2023.1 (January 2023)