Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86.

Isono, Yoshikazu; Sudo, Tomoko; Hoshino, Masami

doi:10.1271/bbb1961.53.1671

Cited by 6 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enzyme was digested by pronase and then incubated with phosphodiesterase. AMP was found in amounts of 3 mol per mol of enzyme by an enzymatic method with myokinase (5). This result suggests that the enzyme contains covalently bound flavin compound, probably flavin adenine dinucleotide (FAD), at 3 mol per mol of enzyme.…”

Section: Resultsmentioning

confidence: 92%

“…Only one enzyme, nucleoside oxidase (EC 1.1.3.28), has been reported to catalyze oxidation of nucleosides. The enzyme from Pseudomonas maltophilia (3)(4)(5)(6) catalyzes the oxidation of nucleosides to the corresponding nucleoside-5Ј-carboxylic acid via nucleoside-5Јaldehyde, using molecular oxygen as a primary electron acceptor, without formation of hydrogen peroxide. The enzyme also shows laccase-like activity in the presence of nucleosides (6).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

Koga¹,

Ogawa²,

Cheng³

et al. 1997

Appl Environ Microbiol

View full text Add to dashboard Cite

A novel enzyme which catalyzes the oxidation of nucleosides to nucleoside-5-carboxylic acids, forming hydrogen peroxide, was purified to homogeneity from Flavobacterium meningosepticum T-2799. The enzyme has a molecular weight of about 500,000, and four nonidentical subunits (molecular weights of 81,000, 69,000, 33,000, and 16,000) were detected on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. On the basis of visible absorption spectra of the purified enzyme, the enzyme is concluded to be a hemoprotein. It also contains covalently bound flavin adenine dinucleotide. The various nucleosides, such as adenosine (K m ‫؍‬ 48 M), inosine (K m ‫؍‬ 66 M), guanosine (K m ‫؍‬ 21 M), thymidine (K m ‫؍‬ 50 M), uridine (K m ‫؍‬ 80 M), and cytidine (K m ‫؍‬ 50 M), were oxidized by the enzyme, but nucleotides, bases, and ribose were not.

show abstract

Section: Resultsmentioning

confidence: 92%

mentioning

confidence: 99%

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

Koga¹,

Ogawa²,

Cheng³

et al. 1997

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Nucleoside oxidase has been reported to be one of the enzymes responsible for the oxidative degradation of nucleosides. The Pseudomonas maltophilia enzyme [1–4] was shown to catalyze the oxidation of nucleosides to the corresponding nucleoside‐5′‐carboxylic acids via nucleoside‐5′‐aldehydes using molecular O 2 as a primary electron acceptor without the formation of H 2 O 2 . Recently, we found another type of nucleoside oxidase in Flavobacterium meningosepticum which produces H 2 O 2 in addition to the reaction products, nucleoside‐5′‐aldehyde and nucleoside‐5′‐carboxylic acid [5].…”

Section: Introductionmentioning

confidence: 99%

Coordinate induction of peroxidase and H₂O₂-forming nucleoside oxidase inFlavobacterium meningosepticum

Koga

Ogawa

Choi

et al. 1999

FEMS Microbiology Letters

View full text Add to dashboard Cite

Flavobacterium meningosepticum produced a peroxidase coordinately with a H2O2‐forming nucleoside oxidase under culture conditions where the bacterium inducibly produced the nucleoside oxidase. The nucleoside oxidase and peroxidase both required Fe2+ or Fe3+ for their production, and Cu2+ enhanced the production of both enzymes. The addition of nucleoside analogs to the medium also enhanced the production of both enzymes. The time course of peroxidase production coincided with that of the nucleoside oxidase production. These results suggest that the peroxidase has a specific function related to the nucleoside oxidase reaction, in breaking down the H2O2 formed, which would otherwise cause oxidative cell damage.

show abstract

Nucleoside oxidase‐modified carbon paste electrode containing quinone: Cathodic current response to nucleosides

et al. 1991

Self Cite

View full text Add to dashboard Cite

The cathodic current for the reduction of benzoquinone at a glassy carbon electrode was increased in the presence of nucleoside oxidase and inosine. This was attributed to the regeneration of benzoquinone from hydroquinone by the laccaselike reaction of the enzyme, the rate of which depended on the concentration of inosine in the solution. Accordingly, an enzyme electrode for nucleosides was constructed by immobilizing nucleoside oxidase behind a dialysis membrane on a carbon paste electrode containing p-benzoquinone or hydroquinone. The current response of the electrode to nucleosides was studied, and the results were discussed on the basis of the laccaselike activity of the enzyme. The nucleoside oxidase-modified electrode was tested as an amperometric enzyme electrode for nucleosides and could be used at least for three weeks.k7W WORDS: Biosensors, nucleosides, nucleoside oxidase. A"TR0DUCTIONConsiderable attention has been given to the coupling of electrode reaction with an enzymatic reaction, in which the substrate of the enzyme can be oxidized or reduced electroenzymatically, i.e., by bioelectrocatalysis [ 1-31. Molecules serving as redox mediators are usually used to achieve the electron transfer coupling, and enzyme electrodes relying on this principle of current response, mediated amperometric enzyme electrodes, have been constructed (4, 51. A variety of redox molecules including redox polymers have been studied for the mediated electron transfer coupling based on glucose oxidase and other oxidoreductases [ 1-31. Similar coupling without mediators has also been reported between ordinary electrodes (such as carbon and metal surfaces), and several kinds of oxidoreductases [ 6-91.This article describes a new type of electroenzymatic coupling different from the above two coupling schemes, which rely on the unique properties of the enzyme used: nucleoside oxidase [NOD] from Pseudomom maltophiria LB-86 (10-131. NOD has a molecular weight of 'To whom correspondence should be addressed. 8 1992 VCH Publishers, Inc. 1040-0397/92/$3.50 + .25 891 892 Ikeda et al.

show abstract

Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86.

Cited by 6 publications

References 0 publications

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

Coordinate induction of peroxidase and H₂O₂-forming nucleoside oxidase inFlavobacterium meningosepticum

Nucleoside oxidase‐modified carbon paste electrode containing quinone: Cathodic current response to nucleosides

Contact Info

Product

Resources

About

Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86.

Cited by 6 publications

References 0 publications

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

Nucleoside Oxidase, a Hydrogen Peroxide-Forming Oxidase, from Flavobacterium meningosepticum

Coordinate induction of peroxidase and H2O2-forming nucleoside oxidase inFlavobacterium meningosepticum

Nucleoside oxidase‐modified carbon paste electrode containing quinone: Cathodic current response to nucleosides

Contact Info

Product

Resources

About

Coordinate induction of peroxidase and H₂O₂-forming nucleoside oxidase inFlavobacterium meningosepticum