Cyanide hydratases and cyanide dihydratases: emerging tools in the biodegradation and biodetection of cyanide
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
PubMed
26329848
DOI
10.1007/s00253-015-6899-0
PII: 10.1007/s00253-015-6899-0
Knihovny.cz E-zdroje
- Klíčová slova
- Cyanide biosensors, Cyanide dihydratase, Cyanide hydratase, Enzyme production, Structure-activity relationships, Wastewater bioremediation,
- MeSH
- Bacteria enzymologie MeSH
- biosenzitivní techniky * MeSH
- biotransformace MeSH
- dehydratasy chemie genetika metabolismus MeSH
- houby enzymologie MeSH
- hydrolasy chemie genetika metabolismus MeSH
- hydrolýza MeSH
- koncentrace vodíkových iontů MeSH
- kyanidy analýza metabolismus MeSH
- látky znečišťující životní prostředí analýza metabolismus MeSH
- mutační analýza DNA MeSH
- mutantní proteiny genetika metabolismus MeSH
- proteinové inženýrství MeSH
- stabilita enzymů MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- cyanide dihydratase MeSH Prohlížeč
- cyanide hydratase MeSH Prohlížeč
- dehydratasy MeSH
- hydrolasy MeSH
- kyanidy MeSH
- látky znečišťující životní prostředí MeSH
- mutantní proteiny MeSH
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.
Citace poskytuje Crossref.org
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