BRENDA - Enzyme Database
show all sequences of 3.5.1.54

Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Balotra, S.; Newman, J.; French, N.G.; Briggs, L.J.; Peat, T.S.; Scott, C.; Acta crystallogr. Sect. F 70, 310-315 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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)
Crystallization
Organism
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.
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467
Pseudomonas sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
6 * 50000, recombinant enzyme, SDS-PAGE
Pseudomonas sp.
360000
-
gel filtration
Pseudomonas sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
allophanate + H2O
Pseudomonas sp.
the reverse reaction is catalyzed by urea carboxylase
2 CO2 + 2 NH3
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
Q936X2
gene atzF
-
Purification (Commentary)
Commentary
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
allophanate + H2O
-
733034
Pseudomonas sp.
2 CO2 + 2 NH3
-
-
-
ir
allophanate + H2O
the reverse reaction is catalyzed by urea carboxylase
733034
Pseudomonas sp.
2 CO2 + 2 NH3
-
-
-
ir
Subunits
Subunits
Commentary
Organism
homohexamer
6 * 50000, recombinant enzyme, SDS-PAGE
Pseudomonas sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
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) (protein specific)
Crystallization
Organism
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.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467
Pseudomonas sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
6 * 50000, recombinant enzyme, SDS-PAGE
Pseudomonas sp.
360000
-
gel filtration
Pseudomonas sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
allophanate + H2O
Pseudomonas sp.
the reverse reaction is catalyzed by urea carboxylase
2 CO2 + 2 NH3
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
allophanate + H2O
-
733034
Pseudomonas sp.
2 CO2 + 2 NH3
-
-
-
ir
allophanate + H2O
the reverse reaction is catalyzed by urea carboxylase
733034
Pseudomonas sp.
2 CO2 + 2 NH3
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
homohexamer
6 * 50000, recombinant enzyme, SDS-PAGE
Pseudomonas sp.
General Information
General Information
Commentary
Organism
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.
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.
General Information (protein specific)
General Information
Commentary
Organism
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.
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.
Other publictions for EC 3.5.1.54
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733179
Balotra
X-ray structure of the amidase ...
Pseudomonas sp.
Appl. Environ. Microbiol.
81
470-480
2015
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733034
Balotra
Crystallization and preliminar ...
Pseudomonas sp.
Acta crystallogr. Sect. F
70
310-315
2014
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2
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733342
Lin
The structure of allophanate h ...
Granulibacter bethesdensis, Granulibacter bethesdensis ATCC BAA-1260
Biochemistry
52
690-700
2013
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1
8
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3
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734220
Fan
Structure and function of allo ...
Kluyveromyces lactis
J. Biol. Chem.
288
21422-21432
2013
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2
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718475
Jacques
The structure of TTHA0988 from ...
no activity in Thermus thermophilus
Acta Crystallogr. Sect. D
67
105-111
2011
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667267
Shapir
Purification and characterizat ...
Enterobacter cloacae, Enterobacter cloacae 99
Appl. Environ. Microbiol.
72
2491-2495
2006
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1
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1
1
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667259
Cheng
Allophanate hydrolase, not ure ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens J14a, Enterobacter cloacae, Enterobacter cloacae 99, Herbaspirillum huttiense, Herbaspirillum huttiense NRRL B-12228, Pseudomonas sp., Ralstonia pickettii, Ralstonia pickettii D
Appl. Environ. Microbiol.
71
4437-4445
2005
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4
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19
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1
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1
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668661
Kanamori
Allophanate hydrolase of Oleom ...
Oleomonas sagaranensis, Oleomonas sagaranensis HD-1
FEMS Microbiol. Lett.
245
61-65
2005
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669098
Shapir
Purification and characterizat ...
Pseudomonas sp.
J. Bacteriol.
187
3731-3738
2005
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6
1
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1
1
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209193
Nishiya
-
Production of urea amidolase b ...
Cyberlindnera jadinii, Cyberlindnera jadinii CA (u)-37
Seibutsu Shiro Bunseki
18
288-293
1995
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1609
Sumrada
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
J. Biol. Chem.
257
9119-9127
1982
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209196
Maitz
-
Purification and properties of ...
Chlamydomonas reinhardtii
Biochim. Biophys. Acta
714
486-491
1982
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5
1
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1602
Whitney
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
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