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Literature summary for 3.5.1.54 extracted from

  • Kanamori, T.; Kanou, N.; Kusakabe, S.; Atomi, H.; Imanaka, T.
    Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea (2005), FEMS Microbiol. Lett., 245, 61-65.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli strain BL21(DE3) Oleomonas sagaranensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.042
-
allophanate pH 9.5, recombinant enzyme Oleomonas sagaranensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
61999
-
2 * 61999, sequence calculation Oleomonas sagaranensis
138000
-
gel filtration, recombinant enzyme Oleomonas sagaranensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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)

Purification (Comment) 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 Comment Organism Reaction ID
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] Comment Organism
108
-
purified recombinant enzyme, substrate allophanate Oleomonas sagaranensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
allophanate + H2O
-
Oleomonas sagaranensis NH3 + CO2
-
ir
allophanate + H2O the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6 Oleomonas sagaranensis NH3 + CO2
-
ir
allophanate + H2O
-
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 Oleomonas sagaranensis HD-1 NH3 + CO2
-
ir

Subunits

Subunits Comment Organism
dimer 2 * 61999, sequence calculation Oleomonas sagaranensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Oleomonas sagaranensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Oleomonas sagaranensis