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Information on EC 3.5.2.15 - cyanuric acid amidohydrolase and Organism(s) Enterobacter cloacae and UniProt Accession P0A3V4

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IUBMB 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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This record set is specific for:
Enterobacter cloacae
UNIPROT: P0A3V4
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The taxonomic range for the selected organisms is: Enterobacter cloacae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cyanuric acid hydrolase, cyanuric acid amidohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyanuric acid hydrolase
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amidase, cyanurate
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cyanurate amidase
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s-triazine ring-cleavage enzyme
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trzD gene product
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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 hide
100785-00-0
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132965-78-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAH_ENTCL
370
0
39420
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized with its natural substrate cyanuric acid by hanging drop, vapor-diffusion experiment in which equal volume of protein (12 mg/ml concentration) and reservoir solution are mixed and allowed to equilibrate against the reservoir at 20 °C. Crystal structure at 2.19 A resolution shows a large displacement of the catalytic lysine (Lys163) in domain 2 away from the active site core, whereas the two other active site lysines from the two other domains are not able to move
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length trzD gene, cloned in pET28b(+)vector6, expressed in Escherichia coli BL21 (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
cyanuric acid hydrolases are of industrial importance because of their use in aquatic recreational facilities to remove cyanuric acid, a stabilizer for the chlorine. Degradation of excess cyanuric acid is necessary to maintain chlorine disinfection in the waters
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bera, A.; Aukema, K.; Elias, M.; Wackett, L.
Structure of the cyanuric acid hydrolase TrzD reveals product exit channel
Sci. Rep.
7
45277
2017
Enterobacter cloacae (P0A3V4)
Manually annotated by BRENDA team