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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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.
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
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
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
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
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
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
no substrates: 1-nitrobiuret, succinamic acid, structurally citrulline, lysine, glutamine, asparagine, and 2-amino-3-propionic acid, and the biuret analog malonamide
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
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
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
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
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
2 * 48120 + 2 * ?, the enzyme forms a stable alpha2beta2 heterotetramer with a the small protein, AtzG, which is required for soluble expression of AtzE
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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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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Enzyme Nomenclature
3.5.1.131 1-carboxybiuret hydrolase
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