BRENDA - Enzyme Database
show all sequences of 3.5.1.54

Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP

Shapir, N.; Sadowsky, M.J.; Wackett, L.P.; J. Bacteriol. 187, 3731-3738 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene atzF, expression of the His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Pseudomonas sp.
Engineering
Amino acid exchange
Commentary
Organism
K91A
site-directed mutagenesis, inactive mutant
Pseudomonas sp.
S165A
site-directed mutagenesis, inactive mutant
Pseudomonas sp.
S189A
site-directed mutagenesis, inactive mutant
Pseudomonas sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
phenyl phosphorodiamidate
-
Pseudomonas sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5
-
allophanate
pH 9.5, recombinant enzyme
Pseudomonas sp.
5.3
-
malonamic acid
pH 9.5, recombinant enzyme
Pseudomonas sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
66223
-
4 * 66223, sequence calculation
Pseudomonas sp.
260000
-
gel filtration, recombinant enzyme
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.
-
NH3 + CO2
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
Q936X2
gene atzF
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Pseudomonas sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pseudomonas sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
allophanate + H2O
-
669098
Pseudomonas sp.
NH3 + CO2
-
-
-
?
allophanate + H2O
-
669098
Pseudomonas sp.
NH3 + CO2
-
-
-
ir
biuret + H2O
-
669098
Pseudomonas sp.
?
-
-
-
?
malonamic acid + H2O
-
669098
Pseudomonas sp.
?
-
-
-
?
malonamic acid + hydroxylamine
hydroxylamine trapping activity
669098
Pseudomonas sp.
malonohydroxamate + ?
-
-
-
?
additional information
substrate specificity, no activity with methyl allophanate, hydantoic acid, oxamic acid, hydroxyurea, methyl carbamate, N-methylurea, acetylurea, 1-acetyl-2-thiourea, and semicarbazide, no activity with rhodanine, rhodanine-3-acetic acid, 3-aminorhodanine, (4R)-(-)-2-thioxo-4-thiazolidinecarboxylic acid, (-)-2-oxo-4-thiazolinecarboxylic acid, and 2-amino-5-bromothiazol
669098
Pseudomonas sp.
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 66223, sequence calculation
Pseudomonas sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.1
-
malonamic acid
pH 9.5, recombinant enzyme
Pseudomonas sp.
16.4
-
allophanate
pH 9.5, recombinant enzyme
Pseudomonas sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
recombinant enzyme
Pseudomonas sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8
11.3
recombinant enzyme
Pseudomonas sp.
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.2
-
phenyl phosphorodiamidate
pH 9.5, recombinant enzyme
Pseudomonas sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
gene atzF, expression of the His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Pseudomonas sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K91A
site-directed mutagenesis, inactive mutant
Pseudomonas sp.
S165A
site-directed mutagenesis, inactive mutant
Pseudomonas sp.
S189A
site-directed mutagenesis, inactive mutant
Pseudomonas sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
phenyl phosphorodiamidate
-
Pseudomonas sp.
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.2
-
phenyl phosphorodiamidate
pH 9.5, recombinant enzyme
Pseudomonas sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5
-
allophanate
pH 9.5, recombinant enzyme
Pseudomonas sp.
5.3
-
malonamic acid
pH 9.5, recombinant enzyme
Pseudomonas sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
66223
-
4 * 66223, sequence calculation
Pseudomonas sp.
260000
-
gel filtration, recombinant enzyme
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.
-
NH3 + CO2
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Pseudomonas sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pseudomonas sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
allophanate + H2O
-
669098
Pseudomonas sp.
NH3 + CO2
-
-
-
?
allophanate + H2O
-
669098
Pseudomonas sp.
NH3 + CO2
-
-
-
ir
biuret + H2O
-
669098
Pseudomonas sp.
?
-
-
-
?
malonamic acid + H2O
-
669098
Pseudomonas sp.
?
-
-
-
?
malonamic acid + hydroxylamine
hydroxylamine trapping activity
669098
Pseudomonas sp.
malonohydroxamate + ?
-
-
-
?
additional information
substrate specificity, no activity with methyl allophanate, hydantoic acid, oxamic acid, hydroxyurea, methyl carbamate, N-methylurea, acetylurea, 1-acetyl-2-thiourea, and semicarbazide, no activity with rhodanine, rhodanine-3-acetic acid, 3-aminorhodanine, (4R)-(-)-2-thioxo-4-thiazolidinecarboxylic acid, (-)-2-oxo-4-thiazolinecarboxylic acid, and 2-amino-5-bromothiazol
669098
Pseudomonas sp.
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 66223, sequence calculation
Pseudomonas sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.1
-
malonamic acid
pH 9.5, recombinant enzyme
Pseudomonas sp.
16.4
-
allophanate
pH 9.5, recombinant enzyme
Pseudomonas sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
recombinant enzyme
Pseudomonas sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8
11.3
recombinant enzyme
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
-
-
1
1
2
-
-
1
-
-
-
1
-
3
-
-
1
-
-
-
-
-
2
3
1
1
-
-
1
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
2
3
1
1
-
-
1
-
-
-
-
2
2
-
-
-
733034
Balotra
Crystallization and preliminar ...
Pseudomonas sp.
Acta crystallogr. Sect. F
70
310-315
2014
-
-
1
1
1
-
-
-
-
-
2
1
-
3
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
733342
Lin
The structure of allophanate h ...
Granulibacter bethesdensis, Granulibacter bethesdensis ATCC BAA-1260
Biochemistry
52
690-700
2013
-
-
1
1
8
-
-
2
-
-
1
2
-
3
-
-
1
-
-
-
-
-
4
1
1
-
-
1
1
-
-
-
-
-
-
-
-
1
-
1
8
-
-
-
-
2
-
-
1
2
-
-
-
1
-
-
-
-
4
1
1
-
-
1
1
-
-
-
-
3
3
-
8
8
734220
Fan
Structure and function of allo ...
Kluyveromyces lactis
J. Biol. Chem.
288
21422-21432
2013
-
-
1
1
3
-
-
-
-
-
-
-
-
3
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
718475
Jacques
The structure of TTHA0988 from ...
no activity in Thermus thermophilus
Acta Crystallogr. Sect. D
67
105-111
2011
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
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-
-
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-
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-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667267
Shapir
Purification and characterizat ...
Enterobacter cloacae, Enterobacter cloacae 99
Appl. Environ. Microbiol.
72
2491-2495
2006
-
-
1
-
-
-
1
1
-
1
3
2
-
6
-
-
-
-
-
-
1
-
10
1
1
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
1
-
1
3
2
-
-
-
-
-
-
1
-
10
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
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
-
-
4
-
-
-
-
-
-
-
-
9
-
18
-
-
-
-
-
-
-
-
19
-
1
-
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
19
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
668661
Kanamori
Allophanate hydrolase of Oleom ...
Oleomonas sagaranensis, Oleomonas sagaranensis HD-1
FEMS Microbiol. Lett.
245
61-65
2005
-
-
1
-
-
-
-
1
-
-
2
2
-
4
-
-
1
1
-
-
1
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
2
2
-
-
-
1
-
-
1
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
669098
Shapir
Purification and characterizat ...
Pseudomonas sp.
J. Bacteriol.
187
3731-3738
2005
-
-
1
-
3
-
1
2
-
-
2
1
-
4
-
-
1
-
-
-
1
-
6
1
-
-
-
2
1
1
-
-
1
-
-
-
-
1
-
-
3
-
-
1
1
2
-
-
2
1
-
-
-
1
-
-
1
-
6
1
-
-
-
2
1
1
-
-
-
-
-
-
-
-
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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2
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1
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1
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1609
Sumrada
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
J. Biol. Chem.
257
9119-9127
1982
-
-
-
-
-
-
-
-
-
-
1
1
-
3
-
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1
-
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2
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1
1
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1
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2
-
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-
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-
-
-
-
-
-
-
-
-
-
209196
Maitz
-
Purification and properties of ...
Chlamydomonas reinhardtii
Biochim. Biophys. Acta
714
486-491
1982
-
-
-
-
-
-
5
1
-
-
2
1
-
1
-
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1
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1
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2
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1
1
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1
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5
1
1
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2
1
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1
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1
-
2
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1602
Whitney
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
-
-
-
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1
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2
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1
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1
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1
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