A Study on p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens
نویسندگان
چکیده
منابع مشابه
Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida.
1. The inducible p-hydroxybenzoate hydroxylase of Pseudomonas putidu which catalyzes the hydroxylation of P-hydroxybenzoate to protocatechuate has been obtained in crystalline form as a protein homogeneous upon ultracentrifugation and electrophoresis. The molecular weight is estimated to be 83,600. 2. The enzyme contains approximately 1 mole of flavin adenine dinucleotide per mole of protein. R...
متن کاملPurification, properties, and oxygen reactivity of p-hydroxybenzoate hydroxylase from Pseudomonas aeruginosa.
The monooxygenase, p-hydroxybenzoate hydroxylase (4-hydroxybenzoate, NADPH:oxygen oxidoreductase (3-hydroxylating), EC 1.14.13.2) has been isolated and purified from Pseudomonas aeruginosa. The reaction catalysed is linked to the pathways for degradation of aromatic compounds by microorganisms. The enzyme has been quantitatively characterized in this paper for use in the mechanistic analysis of...
متن کاملFluoride elimination from substrates in hydroxylation reactions catalyzed by p-hydroxybenzoate hydroxylase.
Several fluorinated derivatives of p-hydroxybenzoate were synthesized and examined as substrates in the reaction catalyzed by p-hydroxybenzoate hydroxylase. All the derivatives tested served as substrates, undergoing tightly coupled hydroxylation by molecular oxygen. Hydroxylation of the difluoro and tetrafluoro derivatives liberated stoichiometric amounts of fluoride. Little or no fluoride was...
متن کاملPseudomonas fluorescens
nas incognita have been previously described as being able to utilize citronellol, geraniol, and linalool (3, 6). Recently, a 50-megadalton (MDa) plasmid has been associated with the degradation of geraniol (9). In this report we describe the isolation of a Pseudomonas fluorescens s train capable of utilizing linalool as a sole carbon and energy source and demonstrate the presence of a transmis...
متن کاملOn the stable enzyme-substrate complex of p-hydroxybenzoate hydroxylase. Evidences for the proton uptake from the substrate.
p-Hydroxybenzoate hydroxylase (EC 1.14.13.2) from Pseudomonas desmolytica is known to form a stable complex with its substrate. Investigations were made on properties of the complex by spectrophotometric measurements and photooxidation. The addition ofp-hydroxybenzoate or benzoate to the oxidized (with respect to bound FAD) enzyme solution caused changes in absorption, fluorescence, and CD spec...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2005
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1982.tb06925.x