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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2002-4-15
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pubmed:abstractText |
Recently, a poplar phloem peroxiredoxin (Prx) was found to accept both glutaredoxin (Grx) and thioredoxin (Trx) as proton donors. To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed. Mutation of the most N-terminal conserved cysteine of Prx (Cys-51) demonstrates that it is the catalytic one. The second cysteine (Cys-76) is not essential for peroxiredoxin activity because the C76A mutant retained approximately 25% of the wild type Prx activity. Only one cysteine of the Grx active site (Cys-27) is essential for peroxiredoxin catalysis, indicating that Grx can act in this reaction either via a dithiol or a monothiol pathway. The creation of covalent heterodimers between Prx and Grx mutants confirms that Prx Cys-51 and Grx Cys-27 are the two residues involved in the catalytic mechanism. The integration of a third cysteine in position 152 of the Prx, making it similar in sequence to the Trx-dependent human Prx V, resulted in a protein that had no detectable activity with Grx but kept activity with Trx. Based on these experimental results, a catalytic mechanism is proposed to explain the Grx- and Trx-dependent activities of poplar Prx.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/GLRX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13609-14
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11832487-Amino Acid Sequence,
pubmed-meshheading:11832487-Blotting, Western,
pubmed-meshheading:11832487-Catalysis,
pubmed-meshheading:11832487-Catalytic Domain,
pubmed-meshheading:11832487-Cloning, Molecular,
pubmed-meshheading:11832487-Cysteine,
pubmed-meshheading:11832487-DNA, Complementary,
pubmed-meshheading:11832487-Dimerization,
pubmed-meshheading:11832487-Dose-Response Relationship, Drug,
pubmed-meshheading:11832487-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11832487-Glutaredoxins,
pubmed-meshheading:11832487-Humans,
pubmed-meshheading:11832487-Hydrogen Peroxide,
pubmed-meshheading:11832487-Kinetics,
pubmed-meshheading:11832487-Molecular Sequence Data,
pubmed-meshheading:11832487-Mutagenesis, Site-Directed,
pubmed-meshheading:11832487-Mutation,
pubmed-meshheading:11832487-Oxidoreductases,
pubmed-meshheading:11832487-Oxygen,
pubmed-meshheading:11832487-Peroxidases,
pubmed-meshheading:11832487-Peroxiredoxins,
pubmed-meshheading:11832487-Protein Binding,
pubmed-meshheading:11832487-Protein Structure, Tertiary,
pubmed-meshheading:11832487-Proteins,
pubmed-meshheading:11832487-Recombinant Proteins,
pubmed-meshheading:11832487-Sequence Homology, Amino Acid,
pubmed-meshheading:11832487-Sulfhydryl Compounds
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pubmed:year |
2002
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pubmed:articleTitle |
Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism.
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pubmed:affiliation |
Unité mixte de recherche IaM INRA-UHP Nancy I, Biochimie et Biologie Moléculaire Végétales, Université Henri Poincaré, 54506 Vandoeuvre Cedex, France.
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pubmed:publicationType |
Journal Article
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