Information on EC 3.5.2.15 - cyanuric acid amidohydrolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.2.15
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RECOMMENDED NAME
GeneOntology No.
cyanuric acid amidohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyanuric acid + H2O = biuret + CO2
show the reaction diagram
involved in a pathway by which the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, is degraded in bacteria
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of cyclic amides
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heterocyclic ring cleavage
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Atrazine degradation
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cyanurate degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
cyanuric acid amidohydrolase
Along with EC 3.5.1.54 (allophanate hydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. This is a key enzyme in the pathway, catalysing the ring cleavage of cyanuric acid. The enzyme is specific for cyanuric acid as substrate as neither the structurally related compounds ammeline (2,4-diamino-6-hydroxy-s-triazine) and ammelide (2-amino-4,6-dihydroxy-s-triazine) nor a number of pyrimidine compounds, such as uracil and cytosine, can act as substrates [3].
CAS REGISTRY NUMBER
COMMENTARY hide
100785-00-0
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132965-78-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 11, NRRLB-15444R
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Manually annotated by BRENDA team
strain 11, NRRLB-15444R
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Manually annotated by BRENDA team
Hormodendrum sp.
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Manually annotated by BRENDA team
strain 90
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Manually annotated by BRENDA team
Penicillium spp.
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cyanuric acid + H2O
biuret + CO2
show the reaction diagram
cyanuric acid + H2O
carboxybiuret
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cyanuric acid + H2O
biuret + CO2
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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; strain A, no effect, no activation by 1 mM Mg2+ or 1 mM Mn2+ as either sulfate or chloride salts
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Barbituric acid
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2,4,6-trihydroxypyrimidine, strong competitive inhibitor, Ki less than 0.0001 mM
Co2+
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strain A, 1 mM: slight inhibition
Cu2+
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strain A, 1 mM: slight inhibition
Fe2+
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strain A, 1 mM: slight inhibition
Zn2+
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strain A, 1 mM: 100fold inhibition
additional information
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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; strain A, no inhibition by 1 mM EDTA, 1 mM Mg2+ or 1 mM Mn2+ as either sulfate or chloride salts
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.11
cyanuric acid
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.6 - 250
cyanuric acid
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100 - 3200
cyanuric acid
2998
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
109.5
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strain A, from recombinant Escherichia coli containing trzD gene
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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strain A
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
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strain A
additional information
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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or pentamer, x * 44000 + x * 33000, the native enzyme has two forms of different sizes: 204000 Da and 160000 Da. Each is a tetramer or pentamer of 44000 Da and 33000 Da subunits, respectively
39400
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strain A, 4 * 39400, calculated from DNA sequence
40000
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strain A, 4 * 40000, SDS-PAGE
44000
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or pentamer, x * 44000 + x * 33000, the native enzyme has two forms of different sizes: 204000 Da and 160000 Da. Each is a tetramer or pentamer of 44000 Da and 33000 Da subunits, respectively
160000
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the native enzyme has two forms of different sizes: 204000 Da and 160000 Da
185000
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strain A, SW300 gel filtration
204000
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the native enzyme has two forms of different sizes: 204000 Da and 160000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for many days, strain D
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, strain D, NRRLB-12228
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strain A, NRRLB-12227, from recombinant Escherichia coli DH5-alpha containing the cloned trzD gene
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
strain 99, cloning large conjugal plasmid pPDL12, carrying the genes encoding the s-triazine degradation pathway, including the trzD gene encoding cyanuric acid amidohydrolase in Klebsiella planticola ATCC 33531, expression in Klebsiella planticola ATCC 33531
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strain 99, trzD gene encoding cyanuric acid amidohydrolase expression in Escherichia coli LE392
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strain A and D, trzD gene encoding cyanuric acid amidohydrolase expression in Escherichia coli LE392
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strain A, expression and overproduction in Escherichia coli DH5-alpha, BRL
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strain A, expression in Escherichia coli LE392
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture