Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis.
Identifieur interne : 000F26 ( Main/Exploration ); précédent : 000F25; suivant : 000F27Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis.
Auteurs : Nicolas Rouhier [France] ; Jean Pierre JacquotSource :
- FEBS letters [ 0014-5793 ] ; 2003.
Descripteurs français
- KwdFr :
- Acide déhydroascorbique (métabolisme), Catalyse (MeSH), Glutarédoxines (MeSH), Liaison aux protéines (MeSH), Neisseria meningitidis (composition chimique), Oxidoreductases (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Peroxydes (métabolisme), Protéines (composition chimique), Protéines (génétique), Protéines (métabolisme), Protéines bactériennes (composition chimique), Protéines bactériennes (génétique), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Structure tertiaire des protéines (MeSH).
- MESH :
- composition chimique : Neisseria meningitidis, Peroxidases, Protéines, Protéines bactériennes, Protéines de fusion recombinantes.
- génétique : Peroxidases, Protéines, Protéines bactériennes, Protéines de fusion recombinantes.
- métabolisme : Acide déhydroascorbique, Peroxidases, Peroxydes, Protéines, Protéines de fusion recombinantes.
- Catalyse, Glutarédoxines, Liaison aux protéines, Oxidoreductases, Peroxirédoxines, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Catalysis (MeSH), Dehydroascorbic Acid (metabolism), Glutaredoxins (MeSH), Neisseria meningitidis (chemistry), Oxidoreductases (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Peroxides (metabolism), Peroxiredoxins (MeSH), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Proteins (chemistry), Proteins (genetics), Proteins (metabolism), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Peroxidases, Proteins, Recombinant Fusion Proteins.
- chemical , genetics : Bacterial Proteins, Peroxidases, Proteins, Recombinant Fusion Proteins.
- chemical , metabolism : Dehydroascorbic Acid, Peroxidases, Peroxides, Proteins, Recombinant Fusion Proteins.
- chemistry : Neisseria meningitidis.
- Catalysis, Glutaredoxins, Oxidoreductases, Peroxiredoxins, Protein Binding, Protein Structure, Tertiary.
Abstract
A hybrid protein from Neisseria meningitidis, which contains both a peroxiredoxin and a glutaredoxin domain, has been isolated. The enzyme was active in the reduction of various peroxides and dehydroascorbate in the presence of reduced glutathione. These findings suggest that both the peroxiredoxin and glutaredoxin domains are biochemically active in the fusion. Moreover, when expressed separately, the glutaredoxin domain was catalytically active and the peroxiredoxin domain possessed a weak activity when supplemented with exogenous glutaredoxin.
DOI: 10.1016/s0014-5793(03)01156-6
PubMed: 14596930
Affiliations:
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Le document en format XML
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The enzyme was active in the reduction of various peroxides and dehydroascorbate in the presence of reduced glutathione. These findings suggest that both the peroxiredoxin and glutaredoxin domains are biochemically active in the fusion. Moreover, when expressed separately, the glutaredoxin domain was catalytically active and the peroxiredoxin domain possessed a weak activity when supplemented with exogenous glutaredoxin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14596930</PMID><DateCompleted><Year>2003</Year><Month>12</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>554</Volume><Issue>1-2</Issue><PubDate><Year>2003</Year><Month>Nov</Month><Day>06</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis.</ArticleTitle><Pagination><MedlinePgn>149-53</MedlinePgn></Pagination><Abstract><AbstractText>A hybrid protein from Neisseria meningitidis, which contains both a peroxiredoxin and a glutaredoxin domain, has been isolated. The enzyme was active in the reduction of various peroxides and dehydroascorbate in the presence of reduced glutathione. These findings suggest that both the peroxiredoxin and glutaredoxin domains are biochemically active in the fusion. Moreover, when expressed separately, the glutaredoxin domain was catalytically active and the peroxiredoxin domain possessed a weak activity when supplemented with exogenous glutaredoxin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>UMR 1136 Interactions Arbres Microorganismes INRA UHP, Faculté des Sciences, P.O. 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