Some Kinetic Properties of 4-Hydroxyphenylpyruvate Dioxygenase from Pseudomonas sp. Strain P.J.874
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چکیده
منابع مشابه
Purification and some properties of human 4-hydroxyphenylpyruvate dioxygenase (I).
4-Hydroxyphenylpyruvate dioxygenase (I-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating), EC 1.13.11.27) has been purified 800-fold in 25% yield from human liver by a procedure involving ammonium sulfate fractionation of an acetone powder extract and chromatography on hydroxylapatite, sulfopropyl-Sephadex C-50, and triethylaminoethyl cellulose. The preparation obtaine...
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One of the three components of the naphthalene dioxygenase occurring in induced cells of Pseudomonas sp. strain NCIB 9816 has been purified to homogeneity. The protein contained 2 g-atoms each of iron and acid-labile sulfur and had an apparent molecular weight of 13,600. The evidence indicates that it is a ferredoxin-type protein that functions as an intermediate electron transfer protein in na...
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4-Chlorophenylacetate 3,4-dioxygenase system from Pseudomonas sp. CBS 3 consists of two protein components, a red-brown iron-sulfur protein (component A) which functions as dioxygenase and an orange-colored reductase (component B). Component B was purified by a five-step procedure. Criterion of purity was sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which also showed that the prot...
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An extracellular phospholipase C was partially purified from Pseudomonas sp. strain KS3.2. The enzyme was composed of an approximately 18-kDa peptide. Maximal enzyme activity was found at pH 7.2 and 50 degrees C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 degrees C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activit...
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Naphthalene dioxygenase (NDO) from Pseudomonas sp. strain NCIB 9816-4 adds both atoms of the dioxygen molecule to styrene to form (R)-l-phenyl-1,2-ethanediol. Product formation is tightly coupled to dioxygen consumption and NADH oxidation. NDO oxidizes styrene-d8 at almost the same initial rate as styrene. The results indicate that dioxygen activation by NDO is different from that by cytochrome...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1983
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1983.tb07514.x