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Enzyme Nomenclature
Information on EC 3.5.1.131 - 1-carboxybiuret hydrolase
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3.5.1.131 1-carboxybiuret hydrolaseIUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex.
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The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtzE
atzEG
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-carboxybiuret + H2O = urea-1,3-dicarboxylate + NH3
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
1-carboxybiuret amidohydrolase
The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex.
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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
1-carboxybiuret + H2O
urea-1,3-dicarboxylate + NH3
-
-
-
?
1-nitrobiuret + H2O
1-nitro-3-carboxyurea + NH3
-
-
-
?
1-carboxybiuret + H2O
1,3-dicarboxyurea + NH3
-
-
-
?
1-carboxybiuret + H2O
1,3-dicarboxyurea + NH3
the product of cyanuric acid hydrolysis by AtzD, 1-carboxybiuret, is the natural substrate for AtzE
-
-
?
1-carboxybiuret + H2O
1,3-dicarboxyurea + NH3
Pseudomonas sp. ADP DSM 11735
the product of cyanuric acid hydrolysis by AtzD, 1-carboxybiuret, is the natural substrate for AtzE
-
-
?
1-carboxymalonamide + H2O
1-carboxymalonamic acid + NH3
-
-
-
?
succinamic acid + H2O
succinic acid + NH3
-
-
-
?
additional information
?
-
purified AtzE has no detectable biuret aminohydrolase activity under any condition tested. No activity with: citrulline, lysine, glutamine, asparagine and 2-amino-3-propionic acid or malonamide
-
-
?
additional information
?
-
Q936X3; A0A384E126
purified AtzE has no detectable biuret aminohydrolase activity under any condition tested. No activity with: citrulline, lysine, glutamine, asparagine and 2-amino-3-propionic acid or malonamide
-
-
?
additional information
?
-
-
purified AtzE has no detectable biuret aminohydrolase activity under any condition tested. No activity with: citrulline, lysine, glutamine, asparagine and 2-amino-3-propionic acid or malonamide
-
-
?
additional information
?
-
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
-
-
?
additional information
?
-
Q936X3; A0A384E126
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
-
-
?
additional information
?
-
-
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
-
-
?
additional information
?
-
Pseudomonas sp. ADP DSM 11735
purified AtzE has no detectable biuret aminohydrolase activity under any condition tested. No activity with: citrulline, lysine, glutamine, asparagine and 2-amino-3-propionic acid or malonamide
-
-
?
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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
1-carboxybiuret + H2O
urea-1,3-dicarboxylate + NH3
-
-
-
?
1-carboxybiuret + H2O
1,3-dicarboxyurea + NH3
the product of cyanuric acid hydrolysis by AtzD, 1-carboxybiuret, is the natural substrate for AtzE
-
-
?
1-carboxybiuret + H2O
1,3-dicarboxyurea + NH3
Pseudomonas sp. ADP DSM 11735
the product of cyanuric acid hydrolysis by AtzD, 1-carboxybiuret, is the natural substrate for AtzE
-
-
?
additional information
?
-
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
-
-
?
additional information
?
-
Q936X3; A0A384E126
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
-
-
?
additional information
?
-
-
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
-
-
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
AtzE forms an alpha2beta2 heterotetramer with a 68-amino acid-long protein (AtzG) encoded in the cyanuric acid mineralization operon from Pseudomonas sp. strain ADP. AtzG is essential for the production of soluble, active AtzE
-
additional information
Q936X3; A0A384E126
AtzE forms an alpha2beta2 heterotetramer with a 68-amino acid-long protein (AtzG) encoded in the cyanuric acid mineralization operon from Pseudomonas sp. strain ADP. AtzG is essential for the production of soluble, active AtzE
-
additional information
-
AtzE forms an alpha2beta2 heterotetramer with a 68-amino acid-long protein (AtzG) encoded in the cyanuric acid mineralization operon from Pseudomonas sp. strain ADP. AtzG is essential for the production of soluble, active AtzE
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.167
1-carboxymalonamide
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
0.785
1-nitrobiuret
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
0.061
1-carboxybiuret
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
0.063
1-carboxybiuret
pH 9.0, temperature not specified in the publication
0.063
1-carboxybiuret
pH 9, 22°C, purified from Pseudomonas sp. ADP
230
1-carboxybiuret
pH 9.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7
1-carboxymalonamide
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
9.4
1-nitrobiuret
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
14.1
1-carboxybiuret
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
15.5
1-carboxybiuret
pH 9.0, temperature not specified in the publication
15.5
1-carboxybiuret
pH 9, 22°C, purified from Pseudomonas sp. ADP
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
42
1-carboxymalonamide
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
12
1-nitrobiuret
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
230
1-carboxybiuret
pH 9, 22°C, recombinant enzyme expressed in Escherichia coli
246
1-carboxybiuret
pH 9, 22°C, purified from Pseudomonas sp. ADP
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q936X3 i.e. catalytic subunit AtzE, and A0A384E126 i.e. accessory subunit AtzG
Q936X3; A0A384E126
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
cyanuric acid is a metabolic intermediate of s-triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is mineralized to ammonia and carbon dioxide by the soil bacterium Pseudomonas sp. strain ADP via three hydrolytic enzymes , AtzD, AtzE, and AtzF
metabolism
Pseudomonas sp. ADP DSM 11735
-
cyanuric acid is a metabolic intermediate of s-triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is mineralized to ammonia and carbon dioxide by the soil bacterium Pseudomonas sp. strain ADP via three hydrolytic enzymes , AtzD, AtzE, and AtzF
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A6J5KH70_9BURK
447
0
46905
TrEMBL
-
A0A6V7BMX1_9XANT
486
0
50451
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
tetramer
2 * 48119, subunit AtzE, 2 * 7422, subunit AtzG, mass spectrometry
heterotetramer
2 * 48120 + 2 * ?, the enzyme forms a stable alpha2beta2 heterotetramer with a the small protein, AtzG, which is required for soluble expression of AtzE
heterotetramer
Pseudomonas sp. ADP DSM 11735
-
2 * 48120 + 2 * ?, the enzyme forms a stable alpha2beta2 heterotetramer with a the small protein, AtzG, which is required for soluble expression of AtzE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of apo AtzE and AtzE bound with the suicide inhibitor phenyl phosphorodiamidate.The AtzE enzyme complex consists of two independent molecules in the asymmetric unit. AtzE forms an alpha2beta2 heterotetramer with 68-amino acid-long protein AtzG. AtzG is essential for the production of soluble, active AtzE. 1-Carboxybiuret binds via hydrogen-bonding interactions. The terminal carboxylate of the substrate binds to Tyr-125, Asn-172, and Gln-402, the main chain carbonyl of Gly-126 binds the terminal adjacent amines, and the main chain NH of Gln-402 binds the carbonyl between those amines
X-ray crystal structures of apo AtzE and AtzE bound with the suicide inhibitor phenyl phosphorodiamidate reveals that the AtzE enzyme complex consists of two independent molecules in the asymmetric unit
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
when AtzE and AtzG are coexpressed in Escherichia coli, a soluble, active enzyme that is catalytically indistinguishable from AtzEG purified from Pseudomonas sp. strain ADP is obtained
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Esquirol, L.; Peat, T.S.; Wilding, M.; Liu, J.W.; French, N.G.; Hartley, C.J.; Onagi, H.; Nebl, T.; Easton, C.J.; Newman, J.; Scott, C.
An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme
J. Biol. Chem.
293
7880-7891
2018
Pseudomonas sp. ADP (Q936X3), Pseudomonas sp. ADP (Q936X3 and A0A384E126), Pseudomonas sp. ADP, Pseudomonas sp. ADP DSM 11735 (Q936X3)
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