Use este identificador para citar ou linkar para este item: https://repositorio.inpa.gov.br/handle/1/15015
Título: Identification of Chromobacterium violaceum genes with potential biotechnological application in environmental detoxification
Autor: 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
Palavras-chave: 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
Data do documento: 2004
Revista: Genetics and Molecular Research
É parte de: 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.
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