Number of the records: 1  

Cyanide hydratases and cyanide dihydratases: emerging tools in the biodegradation and biodetection of cyanide

  1. 1.
    0451731 - MBÚ 2016 RIV DE eng J - Journal Article
    Martínková, Ludmila - Veselá, Alicja Barbara - Rinágelová, Anna - Chmátal, Martin
    Cyanide hydratases and cyanide dihydratases: emerging tools in the biodegradation and biodetection of cyanide.
    Applied Microbiology and Biotechnology. Roč. 99, č. 21 (2015), s. 8875-8882. ISSN 0175-7598. E-ISSN 1432-0614
    R&D Projects: GA TA ČR TA01021368; GA ČR(CZ) GAP504/11/0394
    Institutional support: RVO:61388971
    Keywords : Cyanide hydratase * Cyanide dihydratase * Enzyme production
    Subject RIV: CE - Biochemistry
    Impact factor: 3.376, year: 2015

    The purpose of this study is to summarize the current knowledge of the enzymes which are involved in the hydrolysis of cyanide, i.e., cyanide hydratases (CHTs; EC 4.2.1.66) and cyanide dihydratases (CynD; EC 3.5.5.1). CHTs are probably exclusively produced by filamentous fungi and widely occur in these organisms; in contrast, CynDs were only found in a few bacterial genera. CHTs differ from CynDs in their reaction products (formamide vs. formic acid and ammonia, respectively). Several CHTs were also found to transform nitriles but with lower relative activities compared to HCN. Mutants of CynDs and CHTs were constructed to study the structure-activity relationships in these enzymes or to improve their catalytic properties. The effect of the C-terminal part of the protein on the enzyme activity was determined by constructing the corresponding deletion mutants. CynDs are less active at alkaline pH than CHTs. To improve its bioremediation potential, CynD from Bacillus pumilus was engineered by directed evolution combined with site-directed mutagenesis, and its operation at pH 10 was thus enabled. Some of the enzymes have been tested for their potential to eliminate cyanide from cyanide-containing wastewaters. CynDs were also used to construct cyanide biosensors
    Permanent Link: http://hdl.handle.net/11104/0252836

     
     
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.