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Information on EC 3.5.2.15 - cyanuric acid amidohydrolase and Organism(s) Pseudomonas sp. and UniProt Accession P58329
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3.5.2.15 cyanuric acid amidohydrolaseIUBMB Comments
The enzyme catalyses the ring cleavage of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is highly specific for cyanuric acid. The product was initially thought to be bioret, but was later shown to be 1-carboxybioret.
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Word Map
- 3.5.2.15
- biuret
- agriculture
-
barbituric
- thermoacetica
-
moorella
-
ring-opening
-
swimming
- hydrolases
-
disinfect
- adp
-
herbicide
- melamine
- environmental protection
- ammeline
- atrazine
-
rhodococcus
- ser-lys
-
dyad
-
chlorine
-
acidovorax
- citrulli
-
aminohydrolase
-
acid-degrading
- allophanate
-
tight-binding
- enterobacter
- caulinodans
-
hypochlorite
-
prebiotic
-
azorhizobium
The taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cyanuric acid hydrolase, cyanuric acid amidohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amidase, cyanurate
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-
-
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cyanurate amidase
-
-
-
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s-triazine ring-cleavage enzyme
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-
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trzD gene product
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
cyanuric acid amidohydrolase
The enzyme catalyses the ring cleavage of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is highly specific for cyanuric acid. The product was initially thought to be bioret, but was later shown to be 1-carboxybioret.
CAS REGISTRY NUMBER
COMMENTARY
100785-00-0
-
132965-78-7
-
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
cyanuric acid + H2O
carboxybiuret
-
product spontaneously decarboxylates to give biuret and CO2. Therefore cyanuric acid hydrolase and barbiturase catalyze completely analogous reactions
-
?
cyanuric acid + H2O
biuret + CO2
-
2,4,6-trihydroxy-1,3,5-triazine
-
-
?
cyanuric acid + H2O
biuret + CO2
-
1,3,5-triazine-2,4,6(1H,3H,5H)-trione
-
-
?
cyanuric acid + H2O
biuret + CO2
-
2,4,6-trihydroxy-s-triazine
-
-
?
cyanuric acid + H2O
biuret + CO2
-
heterocyclic ring cleavage
-
-
?
cyanuric acid + H2O
biuret + CO2
-
fourth step in the six-step pathway for metabolism of melamine
-
-
?
cyanuric acid + H2O
biuret + CO2
-
first enzyme of degradative pathway of cyanuric acid
-
-
?
cyanuric acid + H2O
biuret + CO2
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
cyanuric acid + H2O
biuret + CO2
-
herterocyclic ring cleavage
-
-
?
cyanuric acid + H2O
biuret + CO2
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
hypothetical reaction mechanism consistent with a Ser85 nucleophile. Lys42 is a general base, activating Ser85 and promoting formation of a tetrahedral intermediate between Ser85 and the closest substrate carbonyl carbon, this then resolves into the acyl:enzyme intermediate following ring opening. Thereafter, a solvent water molecule is required to hydrolyse the acyl intermediate and regenerate the serine, liberating carboxybiuret
-
-
?
additional information
?
-
-
strain A, no activity with ammeline, 2,4-diamino-6-hydroxy-s-triazine, ammelide, 2-amino-4,6-dihydroxy-s-triazine, uracil, 2,4-dihydroxypyrimidine, 5,6-dihydrouracil, cytosine, 4-amino-2-hydroxypyrimidine, 2,4,5-trihydroxypyrimidine and barbituric acid, 2,4,6-trihydroxypyrimidine
-
-
?
additional information
?
-
-
strain A, high substrate specificity, no activity with any other s-triazine or hydroxypyrimidine compound
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
one step in the six-step pathway for metabolism of melamine
-
-
?
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
cyanuric acid + H2O
biuret + CO2
-
2,4,6-trihydroxy-1,3,5-triazine
-
-
?
cyanuric acid + H2O
biuret + CO2
-
1,3,5-triazine-2,4,6(1H,3H,5H)-trione
-
-
?
cyanuric acid + H2O
biuret + CO2
-
2,4,6-trihydroxy-s-triazine
-
-
?
cyanuric acid + H2O
biuret + CO2
-
fourth step in the six-step pathway for metabolism of melamine
-
-
?
cyanuric acid + H2O
biuret + CO2
-
first enzyme of degradative pathway of cyanuric acid
-
-
?
cyanuric acid + H2O
biuret + CO2
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
cyanuric acid + H2O
biuret + CO2
-
herterocyclic ring cleavage
-
-
?
cyanuric acid + H2O
biuret + CO2
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in a pathway by which herbicides or pesticides based on the symmetrical triazine ring, s-triazine, including atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, are degraded in bacteria
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
involved in metabolism of s-triazine ring structure, component of several important herbicides, including atrazine
-
-
?
additional information
?
-
-
one step in the six-step pathway for metabolism of melamine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
strain A, divalent cations not required, although the possibility that a tightly bound metal ion is present in enzyme cannot be ruled out, no metal analysis of enzyme is performed directly
additional information
-
strain A, no effect, no activation by 1 mM Mg2+ or 1 mM Mn2+ as either sulfate or chloride salts
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Barbituric acid
-
2,4,6-trihydroxypyrimidine, strong competitive inhibitor, Ki less than 0.0001 mM
additional information
-
strain A, no inhibition by 1 mM EDTA, 1 mM Mg2+ or 1 mM Mn2+ as either sulfate or chloride salts
-
additional information
-
strain A, no inhibition by 0.05 mM of ammeline, 2,4-diamino-6-hydroxy-s-triazine, ammelide, 2-amino-4,6-dihydroxy-s-triazine, uracil, 2,4-dihydroxypyrimidine, 5,6-dihydrouracil, cytosine, 4-amino-2-hydroxypyrimidine, 2,4,5-trihydroxypyrimidine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
strain A, kinetic analyses and kinetic data
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Toblerone fold. Product of concatenation of three proteins of YjdF fold. PDB IDs 4BVT, 4BVS, 4BVR, 4BVQ, native enzyme and in complex with melamine, barbituric acid, and cyanuric acid and Xe-derivative, to 1.9, 2.6, 3.1, 2.6 and 2.55 A resolution, respectively. The AtzD monomer, active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential SerLys catalytic dyads. A single catalytic dyad, Ser85Lys42, is hypothesized, based on biochemical evidence and crystallographic data
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
strain A, NRRLB-12227, from recombinant Escherichia coli DH5-alpha containing the cloned trzD gene
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
strain A and D, trzD gene encoding cyanuric acid amidohydrolase expression in Escherichia coli LE392
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
di- and trichloroisocyanuric acids are widely used as water disinfection agents, but cyanuric acid accumulates with repeated additions and must be removed to maintain free hypochlorite for disinfection. The study describes the development of methods for using a cyanuric acid-degrading enzyme contained within nonliving cells that are encapsulated within a porous silica matrix
agriculture
-
cleavage of the s-triazine ring is an important step in the mineralization of s-triazine compounds, extensive used as herbicides or pesticides in agriculture worldwide, and hence in their complete removal from environment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cook, A.M.; Beilstein, P.; Grossenbacher, H.; Hutter, R.
Ring cleavage and degradative pathway of cyanuric acid in bacteria
Biochem. J.
231
25-30
1985
Klebsiella pneumoniae, Klebsiella pneumoniae 99, Pseudomonas sp.
Karns, J.S.
Gene sequence and properties of an s-triazine ring-cleavage enzyme from Pseudomonas sp. strain NRRLB-12227
Appl. Environ. Microbiol.
65
3512-3517
1999
Pseudomonas sp., Pseudomonas sp. A
Eaton, R.W.; Karns, J.S.
Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains
J. Bacteriol.
173
1363-1366
1991
Klebsiella pneumoniae, Klebsiella pneumoniae 99, Pseudomonas sp.
Eaton, R.W.; Karns, J.S.
Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227
J. Bacteriol.
173
1215-1222
1991
Pseudomonas sp., Pseudomonas sp. A
Cook, A.M.
Biodegradation of s-triazine xenobiotics
FEMS Microbiol. Rev.
46
93-116
1987
Gordonia rubripertincta, Gordonia rubripertincta DSM 10347 / NRRLB-15444R, Hormodendrum sp., Klebsiella pneumoniae, Klebsiella pneumoniae 90, Klebsiella pneumoniae 99, Penicillium spp., Pseudomonas sp., Sporothrix schenckii
-
Seffernick, J.L.; Erickson, J.S.; Cameron, S.; Cho, S.; Dodge, A.G.; Richman, J.; Sadowsky, M.J.; Wackett, L.P.
Defining the cyanuric acid hydrolase (AtzD)/barbiturase protein family: Sequences and Reactions
J. Bacteriol.
194
4579-4588
2012
Acidovorax citrulli, Acidovorax citrulli 12227, Moorella thermoacetica, Pseudomonas sp. (P58329)
Peat, T.S.; Balotra, S.; Wilding, M.; French, N.G.; Briggs, L.J.; Panjikar, S., Cowieson, N.; Newman, J.; Scott, C.
Cyanuric acid hydrolase: evolutionary innovation by structural concatenation
Mol. Microbiol.
88
1149-1163
2013
Pseudomonas sp. (P58329)
Yeom, S.; Mutlu, B.; Aksan, A.; Wackett, L.
Bacterial cyanuric acid hydrolase for water treatment
Appl. Environ. Microbiol.
81
6660-6668
2015
Acidovorax citrulli, Acidovorax citrulli 12227, Moorella thermoacetica (Q2RGM7), Pseudomonas sp. (P58329)
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