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Literature summary for 3.5.1.54 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
Search for more literature for 3.5.1.54

Cloned(Commentary)

Cloned (Comment) Organism
gene atzF, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(lambdaDE3) Pseudomonas sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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.
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. Q936X2 gene atzF
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
allophanate + H2O
-
 Pseudomonas sp. 2 CO2 + 2 NH3
-
 ?
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

Subunits Comment Organism
dimer C-terminally truncated enzyme mutant, AtzF467, small-angle X-ray scattering Pseudomonas sp.
homotetramer the full-length wild-type enzyme is a homotetramer in solution, small-angle X-ray scattering Pseudomonas sp.
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

Synonyms Comment Organism
AtzF
-
 Pseudomonas sp.

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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.
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.