Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (721 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
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Paper type: Journal Article,
Impact factor: 3.26, 5-year impact factor: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-4344586909&partnerID=40&md5=d60ad81d897a89232b10ea3a9dd55049
Keywords: Archaea, Protein Disulfide Oxidoreductase, Protein Disulfide-Isomerase, Pyrococcus Furiosus, Redox Sites, Adenosine Triphosphatase, Cation, Mutant Protein, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Archaebacterium, Article, Carboxy Terminal Sequence, Comparative Study, Controlled Study, Enzyme Active Site, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Phylogeny, Nonhuman, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Family, Sequence Homology, Temperature Dependence, Amino Acid Sequence, Animals, Cattle, Circular Dichroism, Cysteine, Insulin, Molecular Sequence Data, Mutation, Nadph Oxidoreductases, Oxidation-Reduction, Ribonucleases, Bacteria (microorganisms), Eukaryota,
Affiliations:
*** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy
Center for Structural Biochemistry, Karolinska Institutet, Huddinge, Sweden
Dipartimento di Chimica Biologica, Univ. Studi di Napoli Federico II, Napoli, Italy
Ist. di Biochimica Delle Proteine, C.N.R., Napoli, Italy
References:
Not available.
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.26, 5-year impact factor: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-4344586909&partnerID=40&md5=d60ad81d897a89232b10ea3a9dd55049
Keywords: Archaea, Protein Disulfide Oxidoreductase, Protein Disulfide-Isomerase, Pyrococcus Furiosus, Redox Sites, Adenosine Triphosphatase, Cation, Mutant Protein, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Archaebacterium, Article, Carboxy Terminal Sequence, Comparative Study, Controlled Study, Enzyme Active Site, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Phylogeny, Nonhuman, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Family, Sequence Homology, Temperature Dependence, Amino Acid Sequence, Animals, Cattle, Circular Dichroism, Cysteine, Insulin, Molecular Sequence Data, Mutation, Nadph Oxidoreductases, Oxidation-Reduction, Ribonucleases, Bacteria (microorganisms), Eukaryota,
Affiliations:
*** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy
Center for Structural Biochemistry, Karolinska Institutet, Huddinge, Sweden
Dipartimento di Chimica Biologica, Univ. Studi di Napoli Federico II, Napoli, Italy
Ist. di Biochimica Delle Proteine, C.N.R., Napoli, Italy
References:
Not available.
Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase
Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol-disulfide exchange reactions with a CXXC sequence motif at their active site. A disulfide oxidoreductase, a highly thermostable protein, was isolated from Pyrococcus furiosus (PfPDO), which is characterized by two redox sites (CXXC) and an unusual molecular mass. Its 3D structure at high resolution suggests that it may be related to the multidomain protein disulfide-isomerase (PDI), which is currently known only in eukaryotes. This work focuses on the functional characterization of PfPDO as well as its relation to the eukaryotic PDIs. Assays of oxidative, reductive, and isomerase activities of PfPDO were performed, which revealed that the archaeal protein not only has oxidative and reductive activity, but also isomerase activity. On the basis of structural data, two single mutants (C35S and C146S) and a double mutant (C35S/C146S) of PfPDO were constructed and analyzed to elucidate the specific roles of the two redox sites. The results indicate that the CPYC site in the C-terminal half of the protein is fundamental to reductive/oxidative activity, whereas isomerase activity requires both active sites. In comparison with PDI, the ATPase activity was tested for PfPDO, which was found to be cation-dependent with a basic pH optimum and an optimum temperature of 90 degreesC. These results and an investigation on genomic sequence databases indicate that PfPDO may be an ancestor of the eukaryotic PDI and belongs to a novel protein disulfide oxidoreductase family.
Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol-disulfide exchange reactions with a CXXC sequence motif at their active site. A disulfide oxidoreductase, a highly thermostable protein, was isolated from Pyrococcus furiosus (PfPDO), which is characterized by two redox sites (CXXC) and an unusual molecular mass. Its 3D structure at high resolution suggests that it may be related to the multidomain protein disulfide-isomerase (PDI), which is currently known only in eukaryotes. This work focuses on the functional characterization of PfPDO as well as its relation to the eukaryotic PDIs. Assays of oxidative, reductive, and isomerase activities of PfPDO were performed, which revealed that the archaeal protein not only has oxidative and reductive activity, but also isomerase activity. On the basis of structural data, two single mutants (C35S and C146S) and a double mutant (C35S/C146S) of PfPDO were constructed and analyzed to elucidate the specific roles of the two redox sites. The results indicate that the CPYC site in the C-terminal half of the protein is fundamental to reductive/oxidative activity, whereas isomerase activity requires both active sites. In comparison with PDI, the ATPase activity was tested for PfPDO, which was found to be cation-dependent with a basic pH optimum and an optimum temperature of 90 degreesC. These results and an investigation on genomic sequence databases indicate that PfPDO may be an ancestor of the eukaryotic PDI and belongs to a novel protein disulfide oxidoreductase family.
Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase
| ▼ Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions |
Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase
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View Export to BibTeX Export to EndNote
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Impact Factor: 1.693
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
21 Records (21 excluding Abstracts).
Total impact factor: 81.925 (81.925 excluding Abstracts).
Total 5 year impact factor: 84.61 (84.61 excluding Abstracts).
Total impact factor: 81.925 (81.925 excluding Abstracts).
Total 5 year impact factor: 84.61 (84.61 excluding Abstracts).
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