<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>39</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Unknown</omics_type><volume>20(12)</volume><submitter>Saez LP</submitter><pubmed_abstract>The alkaliphilic bacterium Pseudomonas pseudoalcaligenes CECT5344 can grow with cyanate, cyanide, or cyanide-containing industrial residues as the sole nitrogen source, but the assimilation of cyanide and cyanate takes place through independent pathways. Therefore, cyanide degradation involves a chemical reaction between cyanide and oxaloacetate to form a nitrile that is hydrolyzed to ammonium by the nitrilase NitC, whereas cyanate assimilation requires a cyanase that catalyzes cyanate decomposition to ammonium and carbon dioxide. The P. pseudoalcaligenes CECT5344 cynFABDS gene cluster codes for the putative transcriptional regulator CynF, the ABC-type cyanate transporter CynABD, and the cyanase CynS. In this study, transcriptional analysis revealed that the structural cynABDS genes constitute a single transcriptional unit, which was induced by cyanate and repressed by ammonium. Mutational characterization of the cyn genes indicated that CynF was essential for cynABDS gene expression and that nitrate/nitrite transporters may be involved in cyanate uptake, in addition to the CynABD transport system. Biodegradation of hazardous jewelry wastewater containing high amounts of cyanide and metals was achieved in a batch reactor operating at an alkaline pH after chemical treatment with hydrogen peroxide to oxidize cyanide to cyanate.</pubmed_abstract><journal>International journal of molecular sciences</journal><pagination>E3008</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6627978</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Cyanate Assimilation by the Alkaliphilic Cyanide-Degrading Bacterium Pseudomonas pseudoalcaligenes CECT5344: Mutational Analysis of the cyn Gene Cluster.</pubmed_title><pmcid>PMC6627978</pmcid><pubmed_authors>Saez LP</pubmed_authors><pubmed_authors>Luque-Almagro VM</pubmed_authors><pubmed_authors>Cabello P</pubmed_authors><pubmed_authors>Roldan MD</pubmed_authors><pubmed_authors>Moreno-Vivian C</pubmed_authors><pubmed_authors>Ibanez MI</pubmed_authors><view_count>39</view_count></additional><is_claimable>false</is_claimable><name>Cyanate Assimilation by the Alkaliphilic Cyanide-Degrading Bacterium Pseudomonas pseudoalcaligenes CECT5344: Mutational Analysis of the cyn Gene Cluster.</name><description>The alkaliphilic bacterium Pseudomonas pseudoalcaligenes CECT5344 can grow with cyanate, cyanide, or cyanide-containing industrial residues as the sole nitrogen source, but the assimilation of cyanide and cyanate takes place through independent pathways. Therefore, cyanide degradation involves a chemical reaction between cyanide and oxaloacetate to form a nitrile that is hydrolyzed to ammonium by the nitrilase NitC, whereas cyanate assimilation requires a cyanase that catalyzes cyanate decomposition to ammonium and carbon dioxide. The P. pseudoalcaligenes CECT5344 cynFABDS gene cluster codes for the putative transcriptional regulator CynF, the ABC-type cyanate transporter CynABD, and the cyanase CynS. In this study, transcriptional analysis revealed that the structural cynABDS genes constitute a single transcriptional unit, which was induced by cyanate and repressed by ammonium. Mutational characterization of the cyn genes indicated that CynF was essential for cynABDS gene expression and that nitrate/nitrite transporters may be involved in cyanate uptake, in addition to the CynABD transport system. Biodegradation of hazardous jewelry wastewater containing high amounts of cyanide and metals was achieved in a batch reactor operating at an alkaline pH after chemical treatment with hydrogen peroxide to oxidize cyanide to cyanate.</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Jun</publication><modification>2024-11-11T19:20:18.147Z</modification><creation>2019-07-30T07:05:57Z</creation></dates><accession>S-EPMC6627978</accession><cross_references><pubmed>31226739</pubmed><doi>10.3390/ijms20123008</doi></cross_references></HashMap>