caa a22 4500 605505675 CHVBK 20210128100623.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s00253-015-6899-0 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6899-0 Cyanide hydratases and cyanide dihydratases: emerging tools in the biodegradation and biodetection of cyanide [Elektronische Daten] [Ludmila Martínková, Alicja Veselá, Anna Rinágelová, Martin Chmátal] 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 pH10 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. Springer-Verlag Berlin Heidelberg, 2015 Cyanide hydratase nationallicence Cyanide dihydratase nationallicence Enzyme production nationallicence Structure-activity relationships nationallicence Wastewater bioremediation nationallicence Cyanide biosensors nationallicence Martínková Ludmila Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut Veselá Alicja Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut Rinágelová Anna Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut Chmátal Martin Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/21(2015-11-01), 8875-8882 0175-7598 99:21<8875 2015 99 253 https://doi.org/10.1007/s00253-015-6899-0 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6899-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Martínková Ludmila Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut NATIONALLICENCE 700 1- Veselá Alicja Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut NATIONALLICENCE 700 1- Rinágelová Anna Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut NATIONALLICENCE 700 1- Chmátal Martin Laboratory of Biotransformation, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20, Prague, Czech Republic aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/21(2015-11-01), 8875-8882 0175-7598 99:21<8875 2015 99 253