BRENDA - Enzyme Database
show all sequences of 3.5.1.54

Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea

Kanamori, T.; Kanou, N.; Kusakabe, S.; Atomi, H.; Imanaka, T.; FEMS Microbiol. Lett. 245, 61-65 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression in Escherichia coli strain BL21(DE3)
Oleomonas sagaranensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.042
-
allophanate
pH 9.5, recombinant enzyme
Oleomonas sagaranensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61999
-
2 * 61999, sequence calculation
Oleomonas sagaranensis
138000
-
gel filtration, recombinant enzyme
Oleomonas sagaranensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
allophanate + H2O
Oleomonas sagaranensis
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
NH3 + CO2
-
-
ir
allophanate + H2O
Oleomonas sagaranensis HD-1
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
NH3 + CO2
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oleomonas sagaranensis
-
isolated from an oil field in Sagara, Japan
-
Oleomonas sagaranensis HD-1
-
isolated from an oil field in Sagara, Japan
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by ultracentrifucation, ion exchange chromatography, and gel filtration, 2.8fold to homogeneity
Oleomonas sagaranensis
Reaction
Reaction
Commentary
Organism
urea-1-carboxylate + H2O = 2 CO2 + 2 NH3
the catalytic triad consists of residues Ser177, Ser153, and Lys79
Oleomonas sagaranensis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
108
-
purified recombinant enzyme, substrate allophanate
Oleomonas sagaranensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
allophanate + H2O
-
668661
Oleomonas sagaranensis
NH3 + CO2
-
-
-
ir
allophanate + H2O
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
668661
Oleomonas sagaranensis
NH3 + CO2
-
-
-
ir
allophanate + H2O
-
668661
Oleomonas sagaranensis HD-1
NH3 + CO2
-
-
-
ir
allophanate + H2O
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
668661
Oleomonas sagaranensis HD-1
NH3 + CO2
-
-
-
ir
Subunits
Subunits
Commentary
Organism
dimer
2 * 61999, sequence calculation
Oleomonas sagaranensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Oleomonas sagaranensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Oleomonas sagaranensis
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in Escherichia coli strain BL21(DE3)
Oleomonas sagaranensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.042
-
allophanate
pH 9.5, recombinant enzyme
Oleomonas sagaranensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61999
-
2 * 61999, sequence calculation
Oleomonas sagaranensis
138000
-
gel filtration, recombinant enzyme
Oleomonas sagaranensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
allophanate + H2O
Oleomonas sagaranensis
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
NH3 + CO2
-
-
ir
allophanate + H2O
Oleomonas sagaranensis HD-1
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
NH3 + CO2
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by ultracentrifucation, ion exchange chromatography, and gel filtration, 2.8fold to homogeneity
Oleomonas sagaranensis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
108
-
purified recombinant enzyme, substrate allophanate
Oleomonas sagaranensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
allophanate + H2O
-
668661
Oleomonas sagaranensis
NH3 + CO2
-
-
-
ir
allophanate + H2O
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
668661
Oleomonas sagaranensis
NH3 + CO2
-
-
-
ir
allophanate + H2O
-
668661
Oleomonas sagaranensis HD-1
NH3 + CO2
-
-
-
ir
allophanate + H2O
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
668661
Oleomonas sagaranensis HD-1
NH3 + CO2
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 61999, sequence calculation
Oleomonas sagaranensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Oleomonas sagaranensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Oleomonas sagaranensis
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1609
Sumrada
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
J. Biol. Chem.
257
9119-9127
1982
-
-
-
-
-
-
-
-
-
-
1
1
-
3
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209196
Maitz
-
Purification and properties of ...
Chlamydomonas reinhardtii
Biochim. Biophys. Acta
714
486-491
1982
-
-
-
-
-
-
5
1
-
-
2
1
-
1
-
-
1
-
-
-
1
-
2
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
5
1
1
-
-
2
1
-
-
-
1
-
-
1
-
2
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1602
Whitney
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-