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Literature summary extracted from

  • Balotra, S.; Newman, J.; French, N.G.; Briggs, L.J.; Peat, T.S.; Scott, C.
    Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP (2014), Acta crystallogr. Sect. F, 70, 310-315.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.54 gene atzF, DNA and amino acid sequence determination and analysis, recombinant expression of functional His-tagged enzyme in Escherichia coli strain BL21 (lambdaDE3) Pseudomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.54 purified full-length wild-type enzyme and truncated mutant enzyme, trypsin-treated AtzF (in situ proteolysis) from 1 M ammonium sulfate, 1 M lithium sulfate, 0.1 M Tris-HCl, pH 8.5, AtzF467 crystals grown from 20% w/v PEG 6000, 0.1 M Na MES pH 6.5, 0.2 M calcium chloride, are used in microseeding for truncated AtzF crystal growth from 11% w/v PEG 3350, 2% Tacsimate, pH 5.0, X-ray diffraction structure determination and analysis at 2.5 A resolution Pseudomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.54 additional information construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467 Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.54 50000
-
 6 * 50000, recombinant enzyme, SDS-PAGE Pseudomonas sp.
3.5.1.54 360000
-
 gel filtration 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. the reverse reaction is catalyzed by urea carboxylase 2 CO2 + 2 NH3
-
 ir

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 active His-tagged enzyme from Escherichia coli strain BL21 (lambdaDE3) by nickel affinity chromatography and gel filtration to about 98% purity and apparent homogeneity 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
-
 ir
3.5.1.54 allophanate + H2O the reverse reaction is catalyzed by urea carboxylase Pseudomonas sp. 2 CO2 + 2 NH3
-
 ir

Subunits

EC Number Subunits Comment Organism
3.5.1.54 homohexamer 6 * 50000, recombinant enzyme, SDS-PAGE Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.5.1.54 AtzF
-
 Pseudomonas sp.

General Information

EC Number General Information Comment Organism
3.5.1.54 evolution allophanate hydrolase is a member of the amidase family of enzymes that possess a conserved serine- and glycine-rich motif, the so-called amidase signature sequence Pseudomonas sp.
3.5.1.54 metabolism allophanate hydrolase also participates in the cyanuric acid mineralization pathway, in which the cyanuric acid ring is hydrolytically opened by cyanuric acid hydrolase (AtzD or TrzD, EC 3.5.2.15) forming the unstable metabolite carboxybiuret, which spontaneously decarboxylates to form biuret. Allophanate is produced from biuret by AtzE (biuret hydrolase; EC 3.5.1.84) via a single deamination. Hydrolysis of allophanate is then carried out by allophanate hydrolase. Both pathways, cyanuric acid mineralization pathway and urea carboxylase pathway, depend upon allophanate deamination by allophanate hydrolase to avoid spontaneous decarboxylation (and urea formation) Pseudomonas sp.