Any feedback?
Information on EC 4.2.1.104 - cyanase and Organism(s) Synechococcus sp. and UniProt Accession Q5N0J1
for references in articles please use BRENDA:EC4.2.1.104Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.1.104 cyanaseIUBMB 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.
Specify your search results
Word Map
- 4.2.1.104
- bicarbonate
-
bicarbonate-dependent
-
anderson
-
fuchs
- pseudoalcaligenes
- molecular biology
- nitrospira
-
decameric
- environmental protection
- biotechnology
- drug development
The taxonomic range for the selected organisms is: Synechococcus sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
cyanase, cyanate hydratase, atcyn, cyanate lyase, oscyn, slr0899, spcyns, cyanate aminohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cyanase
cyanate aminohydrolase
-
-
-
-
cyanate C-N-lyase
-
-
-
-
cyanate hydratase
-
-
-
-
cyanate hydrolase
-
-
-
-
cyanate lyase
Hydrolase, cyanate
-
-
-
-
cyanase
-
-
-
-
cyanate lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyanate + HCO3- + 2 H+ = NH3 + 2 CO2
the enzyme requires bicarbonate as a cofactor. Its mechanism is to catalyse the attack of bicarbonate on cyanate, with elimination of carbon dioxide, thus catalysing hydration of the cyanate to carbamae. The carbamate spontaneously hydrolyses to ammonia and carbon dioxide
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carbon-nitrogen lyase reaction
-
-
-
-
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
37289-24-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NCO- + HCO3- + H+
NH3 + CO2
utilization of exogenous cyanate as a niche source of C and N in cyanobacteria
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NtcA
-
transcription factor, global nitrogen regulator of cyanobacteria, required for expression
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain UTEX625, also known as Synechococcus sp. strain PCC6301
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
transcriptional regulation of cynS expression, overview
additional information
-
transcriptional regulation of cynS expression, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 55
CynS is rapidly inactivated at higher temperatures and only residual activity o f 0.09 U/mg occurs at 50°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant CynS-MBP from Escherichia coli strain HMS174 by amylose affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harano, Y.; Suzuki, I.; Maeda, S.; Kaneko, T.; Tabata, S.; Omata, T.
Identification and nitrogen regulation of the cyanase gene from the cyanobacteria Synechocystis sp. strain PCC 6803 and Synechococcus sp. strain PCC 7942
J. Bacteriol.
179
5744-5750
1997
Synechococcus sp., Synechocystis sp.
Espie, G.S.; Jalali, F.; Tong, T.; Zacal, N.J.; So, A.K.
Involvement of the cynABDS operon and the CO2-concentrating mechanism in the light-dependent transport and metabolism of cyanate by cyanobacteria
J. Bacteriol.
189
1013-1024
2007
Synechococcus elongatus, Synechococcus elongatus (Q59948), Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 (Q59948), Synechococcus sp., Synechococcus sp. (Q5N0J1), Synechococcus sp. UTEX625, Synechocystis sp. (Q55367)
Kamennaya, N.A.; Post, A.F.
Characterization of cyanate metabolism in marine Synechococcus and Prochlorococcus spp
Appl. Environ. Microbiol.
77
291-301
2011
Prochlorococcus sp. (Q7V2U0), Prochlorococcus sp., Prochlorococcus sp. MED4 (Q7V2U0), Synechococcus sp. (A5GPQ6), Synechococcus sp., Synechococcus sp. WH7803 (A5GPQ6)
EXTERNAL LINKS (specific for EC-Number 4.2.1.104)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
