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Literature summary for 1.5.1.37 extracted from

  • Chakraborty, S.; Ortiz-Maldonado, M.; Entsch, B.; Ballou, D.P.
    Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase (2010), Biochemistry, 49, 372-385.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19400
-
deduced from cDNA, without His-tag but with FAD Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the reductase is purified as a stable C-terminally His-tagged yellow protein containing weakly bound FAD Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + NADH + H+ the reductase catalyzes the reduction of FAD by NADH and releases the FADH- product into solution, but unlike the reductase from Actinetobacter baumannii, this catalysis is not influenced by p-hydroxyphenylacetate Pseudomonas aeruginosa FADH2 + NAD+
-
?
FMN + NADH + H+ HpaC can reduce either FAD or FMN Pseudomonas aeruginosa FMNH2 + NAD+
-
?

Subunits

Subunits Comment Organism
monomer gel filtration Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
flavin reductase
-
Pseudomonas aeruginosa
HpaC
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
FAD enzyme solated with some FAD Pseudomonas aeruginosa
NADH no activity with NADPH Pseudomonas aeruginosa