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CNO- + HCO3- + 2 H+
NH3 + 2 CO2
Cyanate + bicarbonate
CO2 + carbamate
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
NCO- + HCO3- + 2 H+
NH3 + 2 CO2
NCO- + HCO3- + H+
NH3 + CO2
NCO- + HCO3- + H+
NH4+ + 2 CO2
NCO- + HCO3- + H+
NH4+ + CO2
additional information
?
-
CNO- + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
CNO- + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + ?
?
-
-
-
?
Cyanate + bicarbonate
?
-
enzyme could play a role in destroying exogenous cyanate originating from the dissociation of carbamoyl compounds such as urea, alternatively cyanate might constitute a convenient nitrogen source for bacteria able to synthesize cyanase in an inducible way
-
-
?
Cyanate + bicarbonate
?
-
breakdown of the inhibitory substance
-
-
?
Cyanate + bicarbonate
?
-
cyanase-deficient strains have increased sensitivity to cyanate and are not able to use cyanate as nitrogen source
-
-
?
Cyanate + bicarbonate
?
-
breakdown of the inhibitory substance
-
-
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
-
-
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
-
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
-
-
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
initial product is carbamate or a related, unstable compound and/or carbamate precursor, which subsequently decomposes to ammonia and bicarbonate
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
ammonia + bicarbonate
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
ammonia + bicarbonate
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
-
-
?
Cyanate + bicarbonate
CO2 + carbamate
-
-
initial product is carbamate or a related, unstable compound and/or carbamate precursor, which subsequently decomposes to ammonia and bicarbonate
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
-
-
-
?
NCO- + HCO3-
NH4+ + CO2
-
-
-
?
NCO- + HCO3-
NH4+ + CO2
-
-
-
?
NCO- + HCO3-
NH4+ + CO2
-
-
-
?
NCO- + HCO3- + 2 H+
NH3 + 2 CO2
-
utilization of CN and SCN as nitrogen sources, cyanase activity present if grown with SCN- and CN-
NH4 and CO2 are terminal nitrogen and carbon products of CN and SCN decomposition
-
?
NCO- + HCO3- + 2 H+
NH3 + 2 CO2
-
utilization of CN and SCN as nitrogen sources, cyanase activity present if grown with SCN- and CN-
NH4 and CO2 are terminal nitrogen and carbon products of CN and SCN decomposition
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
-
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
-
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
utilization of CN- and SCN- as nitrogen sources, cyanase activity present if grown with SCN- and CN-
NH4 and CO2 are terminal nitrogen and carbon products of CN- and SCN- decomposition
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
studies on cyanide and thiocyanate decomposition in Pseudomonas
after supply of CN- and SCN-, production of NH4+ observed at pH 8.8 in phosphate buffer, due to high rate of their utilization as N-source NH3 and CNO are absent from the culture liquids
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
utilization of CN- and SCN- as nitrogen sources, cyanase activity present if grown with SCN- and CN-
NH4 and CO2 are terminal nitrogen and carbon products of CN- and SCN- decomposition
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
studies on cyanide and thiocyanate decomposition in Pseudomonas
after supply of CN- and SCN-, production of NH4+ observed at pH 8.8 in phosphate buffer, due to high rate of their utilization as N-source NH3 and CNO are absent from the culture liquids
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
studies on cyanide and thiocyanate decomposition in Pseudomonas
after supply of CN and SCN, production of NH4+ observed at pH 8.8 in phosphate buffer
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
studies on cyanide and thiocyanate decomposition in Pseudomonas
after supply of CN and SCN, production of NH4+ observed at pH 8.8 in phosphate buffer
-
?
NCO- + HCO3- + H+
NH3 + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
studies on decomposition of externally supplied cyanate, depending on the CynABDS operon, light and internal pools of HCO3- and CO2
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
studies on decomposition of externally supplied cyanate, depending on the CynABDS operon, light and internal pools of HCO3- and CO2
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
studies on decomposition of externally supplied cyanate in photoautotroph cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
studies on decomposition of externally supplied cyanate in cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
cyanase activity in Thiohalophilus thiocyanoxidans, role in thiocyanate decomposition suggested
intermediates carbamate and CO2, spontaneous dissociation into NH3 and CO2
-
?
NCO- + HCO3- + H+
NH3 + CO2
-
thiocyanate metabolism of Thiohalophilus thiocyanoxidans
-
-
?
NCO- + HCO3- + H+
NH4+ + 2 CO2
studies on decomposition of externally supplied cyanate, depending on the CynABDS operon, light and internal pools of HCO3- and CO2
-
-
?
NCO- + HCO3- + H+
NH4+ + 2 CO2
studies on decomposition of externally supplied cyanate, depending on the CynABDS operon, light and internal pools of HCO3- and CO2
-
-
?
NCO- + HCO3- + H+
NH4+ + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
NCO- + HCO3- + H+
NH4+ + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
additional information
?
-
-
activity is induced during growth with cyanide or cyanate, but not with ammonium or nitrate as the nitrogen source
-
-
?
additional information
?
-
no activity in cells grown with ammonium, nitrate, arginine or ornithine as N sources, cyanase of this strain has an assimilatory role but is not essential for cyanide assimilation
-
-
?
additional information
?
-
cyanate is not a key intermediate in the degradation of cyanide, since the cynS mutant is still able to use cyanide as the sole nitrogen source
-
-
?
additional information
?
-
no activity in cells grown with ammonium, nitrate, arginine or ornithine as N sources, cyanase of this strain has an assimilatory role but is not essential for cyanide assimilation
-
-
?
additional information
?
-
cyanate is not a key intermediate in the degradation of cyanide, since the cynS mutant is still able to use cyanide as the sole nitrogen source
-
-
?
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0.01
-
in absence of bicarbonate
0.038
purified recombinant mutant E94L, pH 7.7, 27°C
0.04
purified recombinant mutant S117A, pH 7.7, 27°C
0.047
-
complemented deficient Escherichia coli cells
0.22
-
in the presence of 3 mM bicarbonate and 2 mM cyanate
0.303
purified recombinant enzyme, pH 4.8, 27°C
0.43
purified recombinant enzyme, pH 7.4, 55°C
0.633
purified recombinant enzyme, pH 5.7, 27°C
0.8
purified recombinant enzyme, pH 7.4, 4°C
1666.7
measured by micromol ammonia/mg/s, transgenic Arabidopsis thaliana plants expressing the enzyme, pH and temperature not specified in the publication
2.286
purified recombinant wild-type enzyme, pH 7.7, 27°C
5.56
purified recombinant enzyme, pH 7.4, 26°C
0.75
-
-
0.75
-
activity determined every 15 to 30 min in the presence of 2 mM KCNO and 2 mM HCO3- by formation of NH4+, absent activity if bacteria are grown with NH4 indicates inducible synthesis of cyanase
1.26
-
-
1.26
-
pH optimum 8.1, activity determined every 15 to 30 min in the presence of 2 mM KCNO and 2 mM HCO3- by formation of NH4+, pH values of 7.0, 8.0 and 9.1, absent activity if bacteria are grown with NH4+ indicates inducible synthesis of cyanase
additional information
-
-
additional information
-
strain 21 of Pseudomonas putida is a more active CN decomposer than strain 18 of Pseudomonas stutzeri
additional information
-
strain 21 of Pseudomonas putida is a more active CN decomposer than strain 18 of Pseudomonas stutzeri
additional information
-
cyanase activity shown in whole-cell extracts of the photoautotrophic Synechococcus sp. strain UTEX 625, ability to utilize cyanate-derived CO2 to support photosynthesis affected
additional information
cyanase activity shown in whole-cell extracts of the photoautotrophic Synechococcus sp. strain UTEX 625, ability to utilize cyanate-derived CO2 to support photosynthesis affected
additional information
cyanase activity shown in whole-cell extracts of Synechocystis, high level of cyanase activity when grown with nitrate as N source but unable to utilize exogenous cyanate to support O2 evolution in the light
additional information
-
activity assay in 0.1 M potassium phosphate buffer at pH 7.5 and 37°C with or without 3 mM NaHCO3, cyanate concentration between 0.2 mM and 2 mM, 0.2 to 1 microgram total protein per milliliter, measurement of NH3 formation
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evolution
an ancient gene transfer occurred before the diversification within the Tetranychidae family
evolution
genomic and transcriptomic analysis, phyloegentic analysis, the cyanase gene originates from a single horizontal gene transfer event, which precedes subsequent speciation, comparison of prokaryotic cyanases to eukaryotic cyanase from Tetranychus urticae, which all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure
evolution
phylogenetic relationship of Nitrososphaera gargensis cyanase with the Nitrospira cyanases, overview
evolution
while Nitrososphaera gargensis is the only ammonia-oxidizing microbe with a sequenced genome in which a cyanase is present that is likely acquired from a Nitrospira strain via lateral gene transfer, all nitrite-oxidizers for which a genome sequence is available contain a gene annotated as cyanase. Phylogenetic relationship of Nitrososphaera gargensis cyanase with the Nitrospira cyanases, overview
evolution
-
while Nitrososphaera gargensis is the only ammonia-oxidizing microbe with a sequenced genome in which a cyanase is present that is likely acquired from a Nitrospira strain via lateral gene transfer, all nitrite-oxidizers for which a genome sequence is available contain a gene annotated as cyanase. Phylogenetic relationship of Nitrososphaera gargensis cyanase with the Nitrospira cyanases, overview
-
malfunction
cyanate treatment inhibits germination and early seedling growth of Cyn knockout mutant plants, while wild-type plants show resistance to cyanate stress
malfunction
-
cyanate treatment inhibits germination and early seedling growth of Cyn knockout mutant plants, while wild-type plants show resistance to cyanate stress
-
physiological function
-
the CHa12 peptide derived from cyanate hydratase inhibits the growth of Porphyromonas gingivalis in a dose-dependent manner, cyanate hydratase shows Rgp/Kgp inhibitory activities
physiological function
one role of cyanases in plants is detoxification, plants containing CYN exhibit resistance to KCNO stress
physiological function
one role of cyanases in plants is detoxification, plants containing CYN exhibit resistance to KCNO stress. The conserved residues Ser117 and Glu94 are not only catalytic residues in AtCYN but also contribute to the stability of AtCYN homodecamers. Transcriptional regulation and expression pattern of AtCYN, overview
physiological function
cyanase catalyzes the detoxification of cyanate
physiological function
cyanase enzyme converts cyanate into CO2 and NH3 in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification
physiological function
cyanate hydratase (CynS) catalyzes the decomposition of cyanate and bicarbonate into ammonia and carbon dioxide
physiological function
Nitrospira moscoviensis cells are capable of cyanate degradation in vivo
physiological function
-
one role of cyanases in plants is detoxification, plants containing CYN exhibit resistance to KCNO stress. The conserved residues Ser117 and Glu94 are not only catalytic residues in AtCYN but also contribute to the stability of AtCYN homodecamers. Transcriptional regulation and expression pattern of AtCYN, overview
-
physiological function
-
cyanase enzyme converts cyanate into CO2 and NH3 in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification
-
physiological function
-
cyanate hydratase (CynS) catalyzes the decomposition of cyanate and bicarbonate into ammonia and carbon dioxide
-
additional information
transcriptional regulation of cynS expression, overview
additional information
-
transcriptional regulation of cynS expression, overview
additional information
transcriptional regulation of cynS expression, overview
additional information
-
transcriptional regulation of cynS expression, overview
additional information
ammonia release assay, pigment contents, and total carbohydrate measurements of transgenic Arabidopsis thaliana plants expressing the enzyme, overview. Transgenic Arabidopsis thaliana plants expressing the enzyme are exposed to cyanate, either applied by foliar spray or supplemented in growth medium, and show less reduction in pigment contents, antioxidant enzymes, carbohydrate contents, and reduced levels of plant growth retardation. Plant growth assays under cyanate stress show enhanced growth and biomass accumulation in cyanase overexpressors compared to control plants
additional information
glycerol molecules bound at the entry to the active site of the enzyme during crystallization indicate conserved residues that might be important for the trafficking of substrates and products. The enzyme binds specifically to DNA
additional information
-
glycerol molecules bound at the entry to the active site of the enzyme during crystallization indicate conserved residues that might be important for the trafficking of substrates and products. The enzyme binds specifically to DNA
additional information
the enzyme binds specifically to DNA
additional information
-
the enzyme binds specifically to DNA
additional information
-
transcriptional regulation of cynS expression, overview
-
additional information
-
transcriptional regulation of cynS expression, overview
-
additional information
-
ammonia release assay, pigment contents, and total carbohydrate measurements of transgenic Arabidopsis thaliana plants expressing the enzyme, overview. Transgenic Arabidopsis thaliana plants expressing the enzyme are exposed to cyanate, either applied by foliar spray or supplemented in growth medium, and show less reduction in pigment contents, antioxidant enzymes, carbohydrate contents, and reduced levels of plant growth retardation. Plant growth assays under cyanate stress show enhanced growth and biomass accumulation in cyanase overexpressors compared to control plants
-
additional information
-
glycerol molecules bound at the entry to the active site of the enzyme during crystallization indicate conserved residues that might be important for the trafficking of substrates and products. The enzyme binds specifically to DNA
-
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monomer
19000 recombinant enzyme + His-tag
?
-
x * 17008, calculated from amino acid sequence
?
-
x * 17008, calculated from amino acid sequence
?
-
x * 16362, amino acid sequence calculation
?
x * 50000, recombinant MBP-CynS fusion enzyme, SDS-PAGE
?
-
x * 50000, recombinant MBP-CynS fusion enzyme, SDS-PAGE
-
?
x * 16530, recombinant enzyme, SDS-PAGE
?
-
x * 16530, recombinant enzyme, SDS-PAGE
-
decamer
-
decameric structure required for activity
decamer
-
10 * 17000, SDS-PAGE
decamer
-
10 * 14000, estimated by gel filtration, SDS-PAGE, similar to apparent masses of cyanase of Escherichia coli
homodecamer
10 * 21900, about, sequence calculation, homology modelling of monomers, coimmunoprecipitation, and gel filtration
homodecamer
-
10 * 21900, about, sequence calculation, homology modelling of monomers, coimmunoprecipitation, and gel filtration
-
homodecamer
10 * 22000, about, sequence calculation, homology modelling of monomers, coimmunoprecipitation, and gel filtration
homodecamer
10 * 60000, about, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
octamer
-
8 * 17000, octameric structure required for activity
octamer
-
8 * 17008, crystallographic data
oligomer
-
x * 15200, SDS-PAGE
oligomer
-
8 or 10 * 16350 (4 or 5 disulfide linked dimers), amino acid sequence determination,
oligomer
-
x * 14661, minimum molecular weight calculated from amino acid composition
oligomer
-
x * 15200, SDS-PAGE
-
oligomer
-
x * 14661, minimum molecular weight calculated from amino acid composition
-
additional information
-
the monomers are composed of 2 domains, subunit arrangement, decamer is formed by 5 dimers assembled into a pentamer, model
additional information
CynS protomers form dimers through intricate interactions of their C-terminal domains. Both protomers contribute two beta-strands each to one continuous antiparallel beta-sheet, and the two beta-strands of one protomer are packed against a long alpha-helix from the other protomers within the dimer. Like EcCynS, SpCynS assembles into a ring-like decamer with 5/2 symmetry
additional information
-
CynS protomers form dimers through intricate interactions of their C-terminal domains. Both protomers contribute two beta-strands each to one continuous antiparallel beta-sheet, and the two beta-strands of one protomer are packed against a long alpha-helix from the other protomers within the dimer. Like EcCynS, SpCynS assembles into a ring-like decamer with 5/2 symmetry
additional information
-
CynS protomers form dimers through intricate interactions of their C-terminal domains. Both protomers contribute two beta-strands each to one continuous antiparallel beta-sheet, and the two beta-strands of one protomer are packed against a long alpha-helix from the other protomers within the dimer. Like EcCynS, SpCynS assembles into a ring-like decamer with 5/2 symmetry
-
additional information
prokaryotic and eukaryotic cyanases all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure. Monomer and dimer interfaces analysis, overview
additional information
-
prokaryotic and eukaryotic cyanases all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure. Monomer and dimer interfaces analysis, overview
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E94L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The mutant can form trimers or a mixture of polymers but not decamers
S117A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The mutant can form trimers or a mixture of polymers but not decamers
E94L
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The mutant can form trimers or a mixture of polymers but not decamers
-
S117A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The mutant can form trimers or a mixture of polymers but not decamers
-
E107A
site-directed mutagenesis, soluble, no activity
E107D
site-directed mutagenesis, soluble, no activity
R104A
site-directed mutagenesis, soluble, no activity
R104L
site-directed mutagenesis, soluble, no activity
S130A
site-directed mutagenesis, soluble, no activity
S130T
site-directed mutagenesis, soluble, no activity
additional information
construction of CYN knockout plants
additional information
-
construction of CYN knockout plants
additional information
-
construction of CYN knockout plants
-
additional information
mutant lacking the cynS gene, mutant is unable to use cyanate as the sole nitrogen source but shows the same resistance to cyanate as the wild-type strain, cynS-mutant is not affected in its ability to degrade cyanide, which unambiguously indicates that cyanate is not a central metabolite in cyanide assimilation
additional information
-
mutant lacking the cynS gene, mutant is unable to use cyanate as the sole nitrogen source but shows the same resistance to cyanate as the wild-type strain, cynS-mutant is not affected in its ability to degrade cyanide, which unambiguously indicates that cyanate is not a central metabolite in cyanide assimilation
-
additional information
a delta cyn1 knockout in Sordaria macrospora is totally devoid of cyanase activity and shows an increased sensitivity to exogenously supplied cyanate in an arginine-depleted medium, defects in ascospore germination, but no other obvious morphological phenotype
additional information
-
a delta cyn1 knockout in Sordaria macrospora is totally devoid of cyanase activity and shows an increased sensitivity to exogenously supplied cyanate in an arginine-depleted medium, defects in ascospore germination, but no other obvious morphological phenotype
additional information
Arg104, Glu107 and Ser130 are essential for enzyme activity of the fungal cyanase, irrespectively of substitution by Alanine or another amino-acid
additional information
-
Arg104, Glu107 and Ser130 are essential for enzyme activity of the fungal cyanase, irrespectively of substitution by Alanine or another amino-acid
additional information
-
targeted mutants of Synechococcus elongatus strain PCC7942 disrupted in the coding sequences of the gene encoding the cytosoliyc cyanase (CynS) to study metabolism of exogenously supplied cyanate
additional information
targeted mutants of Synechococcus elongatus strain PCC7942 disrupted in the coding sequences of the gene encoding the cytosoliyc cyanase (CynS) to study metabolism of exogenously supplied cyanate
additional information
-
targeted mutants of Synechococcus elongatus strain PCC7942 impaired in the CO2-concentrating mechanism CCM to study metabolism of exogenously supplied cyanate in cyanobacteria, inactivation of CCM impairs metabolism of external cyanate by insufficient internal pools of HCO3- and CO2 resulting in low levels of the co-substrate bicarbonate that is required for cyanase activity
additional information
targeted mutants of Synechococcus elongatus strain PCC7942 impaired in the CO2-concentrating mechanism CCM to study metabolism of exogenously supplied cyanate in cyanobacteria, inactivation of CCM impairs metabolism of external cyanate by insufficient internal pools of HCO3- and CO2 resulting in low levels of the co-substrate bicarbonate that is required for cyanase activity
additional information
-
targeted mutants of Synechococcus elongatus strain PCC7942, disruption of the cynA gene, encoding a binding protein of a multicomponent ABC-transporter, inactivation of CynA does not affect cyanase function but inhibits decomposition of external cyanate
additional information
targeted mutants of Synechococcus elongatus strain PCC7942, disruption of the cynA gene, encoding a binding protein of a multicomponent ABC-transporter, inactivation of CynA does not affect cyanase function but inhibits decomposition of external cyanate
additional information
-
targeted mutants of Synechococcus elongatus strain PCC7942 disrupted in the coding sequences of the gene encoding the cytosoliyc cyanase (CynS) to study metabolism of exogenously supplied cyanate
-
additional information
-
targeted mutants of Synechococcus elongatus strain PCC7942 impaired in the CO2-concentrating mechanism CCM to study metabolism of exogenously supplied cyanate in cyanobacteria, inactivation of CCM impairs metabolism of external cyanate by insufficient internal pools of HCO3- and CO2 resulting in low levels of the co-substrate bicarbonate that is required for cyanase activity
-
additional information
-
targeted mutants of Synechococcus elongatus strain PCC7942, disruption of the cynA gene, encoding a binding protein of a multicomponent ABC-transporter, inactivation of CynA does not affect cyanase function but inhibits decomposition of external cyanate
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additional information
transfer of the cyanobacterial cyanase into Arabidopsis thaliana plants in order to enhance plant resistance against cyanate toxicity. The recombinant enzyme is active in transgenic plants. Transgenic Arabidopsis thaliana plants expressing the enzyme are exposed to cyanate, either applied by foliar spray or supplemented in growth medium, and show less reduction in pigment contents, antioxidant enzymes, carbohydrate contents, and reduced levels of plant growth retardation. Plant growth assays under cyanate stress show enhanced growth and biomass accumulation in cyanase overexpressors compared to control plants
additional information
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transfer of the cyanobacterial cyanase into Arabidopsis thaliana plants in order to enhance plant resistance against cyanate toxicity. The recombinant enzyme is active in transgenic plants. Transgenic Arabidopsis thaliana plants expressing the enzyme are exposed to cyanate, either applied by foliar spray or supplemented in growth medium, and show less reduction in pigment contents, antioxidant enzymes, carbohydrate contents, and reduced levels of plant growth retardation. Plant growth assays under cyanate stress show enhanced growth and biomass accumulation in cyanase overexpressors compared to control plants
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expressed in Escherichia coli
expressed in Escherichia coli, cyanase gene cynS not arranged in a three-gene cluster
expression in Escherichia coli DH5 alpha
expression in Escherichia coli strain M15
gene Atcyn, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain BL21 (DE3) as His-tagged soluble protein
gene cynS, cynS is presumably transcribed as part of the cynABDS operon, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene cynS, DNA and amino acid sequence determination and analysis
gene cynS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in Escherichia coli strain HMS174 as maltose-binding-protein fusion protein
gene cynS, DNA and amino acid sequence determination and analysis, tightly clustered with 2 genes located upstream, which encode proteins similar to the subunits of nitrate-nitrite transporter, complementation of deficient Escherichia coli strain
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gene cynS, functional recombinant expression of C-terminally His-tagged enzyme in Arabidopsis thaliana plants ecotype Columbia under control of the CaMV 35S promoter via the Agrobacterium tumefaciens (GV3101)-mediated floral dip transformation method, ammonia release assay, pigment contents, and total carbohydrate measurements of transgenic plants, overview
gene cynS, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta (DE3) or Trichoplusia ni High Five cells
gene cynS, tightly clustered with 4 putative molybdenum cofactor biosynthesis genes located downstream
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gene Oscyn, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain BL21 (DE3) as His-tagged soluble protein
gene tetur28g02430, DNA and amino acid sequence determination and analysis, genomic and transcriptomic analysis, phylogenetic analysis, recombinant expression of MBP-tagged or N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene tetur28g02430, sequence comparisons and phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli BL21(DE3) pLys, the Tetranychus urticae cyanase remains functionally active after horizontal gene transfer
expressed in Escherichia coli
expressed in Escherichia coli
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drug development
cyanase is potentially an attractive protein target for the development of acaricides
biotechnology
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analysis of strain characteristics for biotechnological application, detoxification of cyanide- or thiocyanate-containing soils and industrial effluents
biotechnology
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analysis of strain characteristics for biotechnological application, detoxification of cyanide- or thiocyanate-containing soils and industrial effluents
biotechnology
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analysis of strain characteristics for biotechnological application, detoxification of cyanide- or thiocyanate-containing soils and industrial effluents
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biotechnology
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analysis of strain characteristics for biotechnological application, detoxification of cyanide- or thiocyanate-containing soils and industrial effluents
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environmental protection
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potential biotechnological application in environmental detoxification
environmental protection
cyanate and its derivatives are considered as environmental hazardous materials. Cyanate is released to the environment through many chemical industries and mining wastewater. Cyanase enzyme converts cyanate into CO2 and NH3 in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification. But such cyanate biodegradation system is probably insufficient due to the excess cyanate concentrations at contaminated sites. Evaluation of transgenic plant resistance to cyanate stress. The enzyme is a candidate for developing novel ecofriendly phytoremediation systems for cyanate detoxification
environmental protection
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cyanate and its derivatives are considered as environmental hazardous materials. Cyanate is released to the environment through many chemical industries and mining wastewater. Cyanase enzyme converts cyanate into CO2 and NH3 in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification. But such cyanate biodegradation system is probably insufficient due to the excess cyanate concentrations at contaminated sites. Evaluation of transgenic plant resistance to cyanate stress. The enzyme is a candidate for developing novel ecofriendly phytoremediation systems for cyanate detoxification
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molecular biology
analyses of conditions to metabolize exogenously supplied cyanate
molecular biology
analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the Cyn-ABDS operon, light, and on activity of the CO2-concentrating mechanism (CCM), low internal pools of HCO3- and CO2 result in an insufficient supply of bicarbonate
molecular biology
analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the CynABDS operon, light, and on activity of the CO2-concentrating mechanism (CCM), inactivation of the cynS gene leads to inability of decomposition of external cyanate
molecular biology
analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the CynABDS operon, light, and on activity of the CO2-concentrating mechanism (CCM), mutagensis of a periplasmatic binding protein of a multicomponent ABC-transporter (CynA), leads to inability of decomposition of external cyanate due to impaired cyanate uptake, cyanase function is not affected
molecular biology
analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the operon CynABDS, light and internal pools of HCO3- and CO2
molecular biology
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analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the Cyn-ABDS operon, light, and on activity of the CO2-concentrating mechanism (CCM), low internal pools of HCO3- and CO2 result in an insufficient supply of bicarbonate
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molecular biology
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analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the CynABDS operon, light, and on activity of the CO2-concentrating mechanism (CCM), inactivation of the cynS gene leads to inability of decomposition of external cyanate
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molecular biology
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analyses of conditions to metabolize exogenously supplied cyanate, depending on proteins of the CynABDS operon, light, and on activity of the CO2-concentrating mechanism (CCM), mutagensis of a periplasmatic binding protein of a multicomponent ABC-transporter (CynA), leads to inability of decomposition of external cyanate due to impaired cyanate uptake, cyanase function is not affected
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