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Title: | Identification of Chromobacterium violaceum genes with potential biotechnological application in environmental detoxification |
Authors: | Carepo, Marta S.P. Azevedo, Juliana Simão Nina de Porto, Jorge Ivan Rebelo Bentes-Sousa, Alexandra R. Batista, Jacqueline da Silva Silva, Artur L.C. da Schneider, Maria Paula Cruz |
Keywords: | Acid Dehalogenase Arsenic Bacterial Enzyme Cyanate Hydrolase Cyanide Gold Haloacid Unclassified Drug 2 Haloacid Dehalogenase 2 Haloacid Dehalogenase Arsenic Bacterial Protein Hydrolase Amino Acid Sequence Ars Operon Bacterial Gene Biotechnology Catalysis Chromobacterium Chromobacterium Violaceum Conference Paper Cyn Operon Degradation Kinetics Dehalogenation Detoxification Environmental Sanitation Gene Identification Hcn Operon Nonhuman Open Reading Frame Operon Pollution Control Sequence Analysis Antibiotic Resistance Bioremediation Biotechnology Genetics Metabolism Molecular Genetics Nucleotide Sequence Bacteria (microorganisms) Chromobacterium Chromobacterium Violaceum Chromobacterium Violaceum Atcc 12472 Negibacteria Arsenic Bacterial Proteins Base Sequence Biodegradation, Environmental Biotechnology Chromobacterium Cyanides Drug Resistance, Bacterial Hydrolases Molecular Sequence Data Open Reading Frames Operon |
Issue Date: | 2004 |
metadata.dc.publisher.journal: | Genetics and Molecular Research |
metadata.dc.relation.ispartof: | Volume 3, Número 1, Pags. 181-194 |
Abstract: | Chromobacterium violaceum is a Gram-negative bacterium found in a wide variety of tropical and subtropical ecosystems. The complete genome sequence of C. violaceum ATCC 12472 is now available, and it has considerable biotechnological potential for various applications, such as environmental detoxification, as well as medical and agricultural use. We examined the biotechnological potential of C. violaceum for environmental detoxification. Three operons, comprising the ars operon, involved in arsenic resistance, the cyn operon, involved in cyanate detoxification, and the hcn operon, encoding a cyanase, responsible for biogenic production of cyanide, as well as an open reading frame, encoding an acid dehalogenase, were analyzed in detail. Probable catalytic mechanisms for the enzymes were determined, based on amino acid sequence comparisons and on published structural information for these types of proteins. |
Appears in Collections: | Artigos |
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