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Literature summary extracted from

  • Balotra, S.; Newman, J.; Cowieson, N.P.; French, N.G.; Campbell, P.M.; Briggs, L.J.; Warden, A.C.; Easton, C.J.; Peat, T.S.; 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, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(lambdaDE3) Pseudomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.54 purified recombinant wild-type and mutant enzymes, from a reservoir containing 11 to 14% w/v PEG 3350 and 2% Tacsimate reagent, pH 5.0, at 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement Pseudomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.54 H488A site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme below pH 8.0, but slightly reduced activity above pH 8.0 Pseudomonas sp.
3.5.1.54 additional information construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467, the mutant shows similar activity as the wild-type enzyme below pH 8.0, but slightly reduced activity above pH 8.0 Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.54 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas sp.

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.54 recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(lambdaDE3) Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.54 allophanate + H2O
-
 Pseudomonas sp. 2 CO2 + 2 NH3
-
 ?
3.5.1.54 allophanate + H2O the N-terminal domain of allophanate hydrolase deaminates allophanate to produce ammonia and N-carboxycarbamate, while the smaller C-terminal domain seems not to be required for cataytic activity, overview Pseudomonas sp. 2 CO2 + 2 NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.54 dimer C-terminally truncated enzyme mutant, AtzF467, small-angle X-ray scattering Pseudomonas sp.
3.5.1.54 homotetramer the full-length wild-type enzyme is a homotetramer in solution, small-angle X-ray scattering Pseudomonas sp.
3.5.1.54 More AtzF has two main domains: the catalytic domain and a second all-alpha-helical domain that forms the dimer interface. The C-terminal domain has a function in coordinating the quaternary structure of the enzyme. AtzF forms a large, ca. 660-kDa, multienzyme complex with AtzD and AtzE that is capable of mineralizing cyanuric acid Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.5.1.54 AtzF
-
 Pseudomonas sp.

Temperature Optimum [°C]

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

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.54 28 45 maximal activity at 28°C, 50% of maximal activity at 45°C Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.54 7 9.5 assay at Pseudomonas sp.

General Information

EC Number General Information Comment Organism
3.5.1.54 evolution the positions of the amino acids essential for catalysis (Ser165, Ser189, and Lys91) and substrate binding (Tyr320 and Arg328), are highly conserved Pseudomonas sp.
3.5.1.54 additional information the N-terminal amidase domain of the enzyme reveals that it is highly homologous to allophanate hydrolases involved in a different catabolic process in other organisms (i.e., the mineralization of urea), structure analysis, overview. The smaller C-terminal domain does not appear to have a physiologically relevant catalytic function. AtzF forms a large, ca. 660-kDa, multienzyme complex with AtzD and 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. The positions of the amino acids essential for catalysis (Ser165, Ser189, and Lys91) and substrate binding (Tyr320 and Arg328), are highly conserved Pseudomonas sp.