Purification and Properties of 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 کاملPurification and properties of nucleoside hydrolase from Pseudomonas fluorescens.
An enzyme which catalyzes the hydrolytic cleavage of various ribonucleosides to free base and ribose components has been obtained from cells of Pseudomonas fluorescens and purified about 300-fold by fractionation with protamine sulfate, ammonium sulfate, alumina Cy, and diethylaminoethyl cellulose. The preparation thus purEed catalyzes the hydrolysis of about 50 moles of uridine per min per mg ...
متن کاملPurification and characteristics of aspartate transcarbamylase from Pseudomonas fluorescens.
Aspartate transcarbamylase from a Pseudomonas fluerescens has been purified to homogeneity. The enzyme has a molecular weight of 360,000. It is composed of 2 apparently identical subunits with molecular weights of 180,000. Activity can be recovered from the enzyme denatured with mercaptoethanol and sodium dodecyl sulfate when the dodecyl sulfate is dialyzed away. The renatured enzyme has the mo...
متن کاملPurification and some properties of proteinase from Pseudomonas fluorescens No. 33.
The extracellular proteinase from Pseudomonas fluorescens No. 33 was purified to electrophoretic homogeneity by a procedure including precipitation with HCl and (NH4)2SO4, and column chromatography. The enzyme was purified 170-fold giving a yield of 7% of the original activity. The molecular mass of the purified enzyme was 48,000 by SDS-PAGE. The optimum pH and temperature for the hydrolysis of...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45081-3