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Information on EC 4.2.1.104 - cyanase and Organism(s) Arabidopsis thaliana and UniProt Accession O22683

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.104 cyanase
IUBMB Comments
This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen [6,7]. Reaction (1a) can be considered an equivalent of 'cyanate + H2O = carbamate', where the water molecule is provided by the dehydration of bicarbonate to carbon dioxide , and hence the enzyme is classified as a hydrolase.
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Arabidopsis thaliana
UNIPROT: O22683
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
+
2
=
+
2
+
+
2
=
+
2
Synonyms
cyanase, cyanate hydratase, atcyn, cyanate lyase, oscyn, slr0899, spcyns, cyanate aminohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyanate hydrolase
-
cyanase
-
-
-
-
cyanate aminohydrolase
-
-
-
-
cyanate C-N-lyase
-
-
-
-
cyanate hydratase
-
-
-
-
cyanate hydrolase
-
-
-
-
cyanate lyase
-
-
-
-
Hydrolase, cyanate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbon-nitrogen lyase reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
carbamate hydro-lyase
This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen [6,7]. Reaction (1a) can be considered an equivalent of 'cyanate + H2O = carbamate', where the water molecule is provided by the dehydration of bicarbonate to carbon dioxide [2], and hence the enzyme is classified as a hydrolase.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-24-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cyanate + HCO3- + 2 H+
NH3 + 2 CO2
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.038
purified recombinant mutant E94L, pH 7.7, 27°C
0.04
purified recombinant mutant S117A, pH 7.7, 27°C
2.286
purified recombinant wild-type enzyme, pH 7.7, 27°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 8.8
over 75% of maximal activity at pH 6.7-8.8, no activity at pH 5.7 and pH 4.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19 - 34
the enzyme activity increases concomitantly with increasing temperature, the activity is 2fold higher at 34°C compared to 19°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the transcription level of AtCYN is higher in the flower than in other organs of Arabidopsis thaliana
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CYNS_ARATH
168
0
18592
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21900
10 * 21900, about, sequence calculation, homology modelling of monomers, coimmunoprecipitation, and gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodecamer
10 * 21900, about, sequence calculation, homology modelling of monomers, coimmunoprecipitation, and gel filtration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged soluble CYN from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Atcyn, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain BL21 (DE3) as His-tagged soluble protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtCYN transcription is not significantly affected by KCNO treatment, but is induced by salt stress
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Qian, D.; Jiang, L.; Lu, L.; Wei, C.; Li, Y.
Biochemical and structural properties of cyanases from Arabidopsis thaliana and Oryza sativa
PLoS ONE
6
e18300
2011
Arabidopsis thaliana (O22683), Arabidopsis thaliana, Arabidopsis thaliana Col 0 (O22683), Oryza sativa (Q9FWK4), Oryza sativa
Manually annotated by BRENDA team