MersV1, PubMed, Curation, bibRecord, 002626

Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus.

Identifieur interne : 002626 ( PubMed/Curation ); précédent : 002625; suivant : 002627

Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus.

Auteurs : K. Kitano [Japon] ; Y. Niimura ; Y. Nishiyama ; K. Miki

Source :

Journal of biochemistry [ 0021-924X ] ; 1999.

RBID : pubmed:10423523

Descripteurs français

English descriptors

KwdEn :
- Ammonium Sulfate (metabolism), Bacteria (enzymology), Chromatography, Gel, Crystallography, X-Ray, Enzyme Activation, Models, Molecular, Molecular Weight, Multienzyme Complexes (metabolism), NADH, NADPH Oxidoreductases (metabolism), Osmolar Concentration, Peroxidase (metabolism), Peroxidases (chemistry), Peroxidases (metabolism), Peroxiredoxins, Phosphates (metabolism), Potassium Chloride (metabolism), Potassium Compounds (metabolism), Scattering, Radiation, Sulfates (metabolism).
MESH :
- chemical , chemistry : Peroxidases.
- chemical , metabolism : Ammonium Sulfate, Multienzyme Complexes, NADH, NADPH Oxidoreductases, Peroxidase, Peroxidases, Phosphates, Potassium Chloride, Potassium Compounds, Sulfates.
- enzymology : Bacteria.
- Chromatography, Gel, Crystallography, X-Ray, Enzyme Activation, Models, Molecular, Molecular Weight, Osmolar Concentration, Peroxiredoxins, Scattering, Radiation.

Abstract

AhpC protein, purified from Amphibacillus xylanus with a molecular mass of 20.8 kDa, protects cells against oxidation damage. The enzyme catalyses the reduction of hydroperoxides in cooperation with the 55 kDa flavoprotein, A. xylanus NADH oxidase (NADH oxidase-AhpC system). A. xylanus AhpC has two disulfide linkages between monomers and can act in the homodimer form. Gel-filtration column chromatography and dynamic light scattering (DLS) suggest that A. xylanus AhpC also forms a large oligomeric assembly (10-12 mers). A. xylanus AhpC was crystallized and X-ray diffraction data were collected to 3.0 A. The self-rotation function revealed fivefold and twofold axes located perpendicularly to each other, suggesting that the molecular assembly of A. xylanus AhpC is composed of ten monomers. The oligomerization of A. xylanus AhpC is affected by ionic strength in the DLS measurements. The H(2)O(2) reductase activity of the A. xylanus NADH oxidase-AhpC system is also affected by ionic strength, and it was found that the decamerization of AhpC might be required for the activation of the NADH oxidase-AhpC system.

DOI: 10.1093/oxfordjournals.jbchem.a022451
PubMed: 10423523

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Le document en format XML

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<author><name sortKey="Kitano, K" sort="Kitano, K" uniqKey="Kitano K" first="K" last="Kitano">K. Kitano</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.</nlm:affiliation>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-8502</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Niimura, Y" sort="Niimura, Y" uniqKey="Niimura Y" first="Y" last="Niimura">Y. Niimura</name>
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<author><name sortKey="Nishiyama, Y" sort="Nishiyama, Y" uniqKey="Nishiyama Y" first="Y" last="Nishiyama">Y. Nishiyama</name>
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<author><name sortKey="Miki, K" sort="Miki, K" uniqKey="Miki K" first="K" last="Miki">K. Miki</name>
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<author><name sortKey="Nishiyama, Y" sort="Nishiyama, Y" uniqKey="Nishiyama Y" first="Y" last="Nishiyama">Y. Nishiyama</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Ammonium Sulfate (metabolism)</term>
<term>Bacteria (enzymology)</term>
<term>Chromatography, Gel</term>
<term>Crystallography, X-Ray</term>
<term>Enzyme Activation</term>
<term>Models, Molecular</term>
<term>Molecular Weight</term>
<term>Multienzyme Complexes (metabolism)</term>
<term>NADH, NADPH Oxidoreductases (metabolism)</term>
<term>Osmolar Concentration</term>
<term>Peroxidase (metabolism)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (metabolism)</term>
<term>Peroxiredoxins</term>
<term>Phosphates (metabolism)</term>
<term>Potassium Chloride (metabolism)</term>
<term>Potassium Compounds (metabolism)</term>
<term>Scattering, Radiation</term>
<term>Sulfates (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique</term>
<term>Bactéries (enzymologie)</term>
<term>Chlorure de potassium (métabolisme)</term>
<term>Chromatographie sur gel</term>
<term>Complexes multienzymatiques (métabolisme)</term>
<term>Composés du potassium (métabolisme)</term>
<term>Concentration osmolaire</term>
<term>Cristallographie aux rayons X</term>
<term>Diffusion de rayonnements</term>
<term>Masse moléculaire</term>
<term>Modèles moléculaires</term>
<term>Myeloperoxidase (métabolisme)</term>
<term>NADH, NADPH oxidoreductases (métabolisme)</term>
<term>Peroxidases ()</term>
<term>Peroxidases (métabolisme)</term>
<term>Peroxirédoxines</term>
<term>Phosphates (métabolisme)</term>
<term>Sulfate d'ammonium (métabolisme)</term>
<term>Sulfates (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ammonium Sulfate</term>
<term>Multienzyme Complexes</term>
<term>NADH, NADPH Oxidoreductases</term>
<term>Peroxidase</term>
<term>Peroxidases</term>
<term>Phosphates</term>
<term>Potassium Chloride</term>
<term>Potassium Compounds</term>
<term>Sulfates</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bactéries</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacteria</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chlorure de potassium</term>
<term>Complexes multienzymatiques</term>
<term>Composés du potassium</term>
<term>Myeloperoxidase</term>
<term>NADH, NADPH oxidoreductases</term>
<term>Peroxidases</term>
<term>Phosphates</term>
<term>Sulfate d'ammonium</term>
<term>Sulfates</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term>
<term>Crystallography, X-Ray</term>
<term>Enzyme Activation</term>
<term>Models, Molecular</term>
<term>Molecular Weight</term>
<term>Osmolar Concentration</term>
<term>Peroxiredoxins</term>
<term>Scattering, Radiation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Chromatographie sur gel</term>
<term>Concentration osmolaire</term>
<term>Cristallographie aux rayons X</term>
<term>Diffusion de rayonnements</term>
<term>Masse moléculaire</term>
<term>Modèles moléculaires</term>
<term>Peroxidases</term>
<term>Peroxirédoxines</term>
</keywords>
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<front><div type="abstract" xml:lang="en">AhpC protein, purified from Amphibacillus xylanus with a molecular mass of 20.8 kDa, protects cells against oxidation damage. The enzyme catalyses the reduction of hydroperoxides in cooperation with the 55 kDa flavoprotein, A. xylanus NADH oxidase (NADH oxidase-AhpC system). A. xylanus AhpC has two disulfide linkages between monomers and can act in the homodimer form. Gel-filtration column chromatography and dynamic light scattering (DLS) suggest that A. xylanus AhpC also forms a large oligomeric assembly (10-12 mers). A. xylanus AhpC was crystallized and X-ray diffraction data were collected to 3.0 A. The self-rotation function revealed fivefold and twofold axes located perpendicularly to each other, suggesting that the molecular assembly of A. xylanus AhpC is composed of ten monomers. The oligomerization of A. xylanus AhpC is affected by ionic strength in the DLS measurements. The H(2)O(2) reductase activity of the A. xylanus NADH oxidase-AhpC system is also affected by ionic strength, and it was found that the decamerization of AhpC might be required for the activation of the NADH oxidase-AhpC system.</div>
</front>
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<DateCompleted><Year>1999</Year>
<Month>12</Month>
<Day>13</Day>
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<DateRevised><Year>2019</Year>
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<Title>Journal of biochemistry</Title>
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<ArticleTitle>Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus.</ArticleTitle>
<Pagination><MedlinePgn>313-9</MedlinePgn>
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<Abstract><AbstractText>AhpC protein, purified from Amphibacillus xylanus with a molecular mass of 20.8 kDa, protects cells against oxidation damage. The enzyme catalyses the reduction of hydroperoxides in cooperation with the 55 kDa flavoprotein, A. xylanus NADH oxidase (NADH oxidase-AhpC system). A. xylanus AhpC has two disulfide linkages between monomers and can act in the homodimer form. Gel-filtration column chromatography and dynamic light scattering (DLS) suggest that A. xylanus AhpC also forms a large oligomeric assembly (10-12 mers). A. xylanus AhpC was crystallized and X-ray diffraction data were collected to 3.0 A. The self-rotation function revealed fivefold and twofold axes located perpendicularly to each other, suggesting that the molecular assembly of A. xylanus AhpC is composed of ten monomers. The oligomerization of A. xylanus AhpC is affected by ionic strength in the DLS measurements. The H(2)O(2) reductase activity of the A. xylanus NADH oxidase-AhpC system is also affected by ionic strength, and it was found that the decamerization of AhpC might be required for the activation of the NADH oxidase-AhpC system.</AbstractText>
</Abstract>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus.

Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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