4.2.1.104: cyanase
This is an abbreviated version!
For detailed information about cyanase, go to the full flat file.
Word Map on EC 4.2.1.104
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4.2.1.104
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bicarbonate
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bicarbonate-dependent
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anderson
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fuchs
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pseudoalcaligenes
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molecular biology
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nitrospira
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decameric
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environmental protection
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biotechnology
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drug development
- 4.2.1.104
- bicarbonate
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bicarbonate-dependent
-
anderson
-
fuchs
- pseudoalcaligenes
- molecular biology
- nitrospira
-
decameric
- environmental protection
- biotechnology
- drug development
Reaction
Synonyms
107368746, AtCYN, cyanase, cyanate aminohydrolase, cyanate C-N-lyase, cyanate hydratase, cyanate hydrolase, cyanate lyase, CYN, CynS, EC 3.5.5.3, EC 4.3.99.1, Hydrolase, cyanate, Ngar_c31480, NITMOv2_1274, OsCYN, slr0899, SpCynS, Spro_1533, tetur28g02430
ECTree
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Engineering
Engineering on EC 4.2.1.104 - cyanase
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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
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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
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S117A
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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
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additional information
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
Pseudomonas oleovorans CECT 5344
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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
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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
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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
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Arg104, Glu107 and Ser130 are essential for enzyme activity of the fungal cyanase, irrespectively of substitution by Alanine or another amino-acid
additional information
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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
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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
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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
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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
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additional information
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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
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additional information
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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
Synechocystis sp. PCC 6803 Kazusa
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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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