Identification of Chromobacterium violaceum genes with potential biotechnological application in environmental detoxification

• Author(s): 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
• Date: 2020
• Origin: Oasisbr
• Subject(s): 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
• Document Type: Journal article
• Language: English

Description

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.