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Literature summary for 3.5.1.54 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
Search for more literature for 3.5.1.54

Cloned(Commentary)

Cloned (Comment) Organism
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)

Crystallization (Comment) Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. ADP Q936X2
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
urea-1-carboxylate + H2O
-
 Pseudomonas sp. ADP 2 CO2 + 2 NH3
-
 ?

Subunits

Subunits Comment Organism
dimer N-terminal enzyme amidase domain AtzF467 Pseudomonas sp. ADP
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

Synonyms Comment Organism
AtzF
-
 Pseudomonas sp. ADP

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

General Information Comment Organism
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
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