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Literature summary extracted from

  • Balotra, S.; Newman, J.; Cowieson, N.; French, N.; Campbell, P.; Briggs, L.; Warden, A.; Easton, C.; Peat, T.; Scott, C.
    X-Ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex (2015), Appl. Environ. Microbiol., 81, 470-480 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.54 gene atzF, sequence comparisons, cloning of atzF and the truncated gene encoding the amidase (N-terminal) domain of AtzF (atzF467), recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Pseudomonas sp. ADP

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.54 purified recombinant amidase domain of allophanate hydrolase, AtzF467, X-ray diffraction structure determinations and analysis at 2.5 A resolution Pseudomonas sp. ADP

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.54 H488A site-directed mutagenesis Pseudomonas sp. ADP

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.54 urea-1-carboxylate + H2O Pseudomonas sp. ADP
-
 2 CO2 + 2 NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.54 Pseudomonas sp. ADP Q936X2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.54 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Pseudomonas sp. ADP

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.54 additional information the catalytic reaction is catalyzed by either the full-length AtzF or the amidase domain of AtzF, AtzF467. There is no catalytic advantage conferred by the C terminus of AtzF in vitro Pseudomonas sp. ADP ?
-
 ?
3.5.1.54 urea-1-carboxylate + H2O
-
 Pseudomonas sp. ADP 2 CO2 + 2 NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.54 dimer N-terminal enzyme amidase domain AtzF467 Pseudomonas sp. ADP
3.5.1.54 More structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, ca. 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE. Analysis of the multimerization of AtzF and Atzf467 by small-angle x-ray scattering (SAXS) Pseudomonas sp. ADP

Synonyms

EC Number Synonyms Comment Organism
3.5.1.54 AtzF
-
 Pseudomonas sp. ADP

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.54 28
-
 assay at Pseudomonas sp. ADP

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.54 8 8.5 assay at Pseudomonas sp. ADP

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.54 additional information
-
 at pH 7, there is no significant difference in the residual activities recovered for AtzF, AtzF467, and AtzF H488A, but at pH 9.0, the apparent melting temperature (Tm) for AtzF467 is reduced from 44°C to 41°C, and although the apparent Tm for AtzF H488A is 45°C, it is lower than that for AtzF by nearly 1.5°C Pseudomonas sp. ADP

General Information

EC Number General Information Comment Organism
3.5.1.54 additional information structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, about 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE that is capable of mineralizing cyanuric acid. The function of this complex may be to channel substrates from one active site to the next, effectively protecting unstable metabolites, such as allophanate, from solvent-mediated decarboxylation to a dead-end metabolic product. There is no catalytic advantage conferred by the C terminus of AtzF in vitro Pseudomonas sp. ADP
3.5.1.54 physiological function the activity of the allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, provides the final hydrolytic step for the mineralization of s-triazines, such as atrazine and cyanuric acid. The action of AtzF provides metabolic access to two of the three nitrogens in each triazine ring Pseudomonas sp. ADP