http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11474
A novel chimera: the \"truncated hemoglobin-antibiotic monooxygenase\" from Streptomyces avermitilis. (Articolo in rivista)
- Type
- Label
- A novel chimera: the \"truncated hemoglobin-antibiotic monooxygenase\" from Streptomyces avermitilis. (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.gene.2007.01.038 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Bonamore A; Attili A; Arenghi F; Catacchio B; Chiancone E; Morea; Boffi A (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- PubMe (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Biochemical Sciences, University of Rome \"La Sapienza\", P.le Aldo Moro 5, 00185 Rome, Italy;
Istituto Nazionale di Fisica Nucleare, via P. Giuria 1, 10125 Torino, Italy;
CPC Biotech srl. Via dei Mille 74, 80121 Napoli, Italy;
CNR Institute of Molecular Biology and Pathology, University of Rome \"La Sapienza\", P.le Aldo Moro 5, 00185 Rome, Italy; (literal)
- Titolo
- A novel chimera: the \"truncated hemoglobin-antibiotic monooxygenase\" from Streptomyces avermitilis. (literal)
- Abstract
- Novel chimeric proteins made of a globin domain fused with a \"cofactor free\" monooxygenase domain have been identified within the Streptomyces avermitilis and Frankia sp. genomes by means of bioinformatics methods. Structure based sequence alignments show that the globin domains of both proteins can be unambiguously assigned to the truncated hemoglobin family, in view of the, striking similarity to the truncated hemoglobins from Mycobacterium tuberculosis, Thermobifida fusca and Bacillus subtilis. In turn, the non-heme domains belong to a family of small (about 100 aminoacids) homodimeric proteins annotated as antibiotic biosynthesis monooxygenases, despite the lack of a cofactor (e.g., a metal, a flavin or a heme) necessary for oxygen activation. (literal)
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- Autore CNR
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