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Literature summary extracted from

  • Schneider, J.; Kaltwasser, H.
    Urease from Arthrobacter oxydans, a nickel-containing enzyme (1984), Arch. Microbiol., 139, 355-360.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.5 12.5
-
 Urea
-
 Pseudarthrobacter oxydans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.5 Nickel nickel metalloenzyme Pseudarthrobacter oxydans
3.5.1.5 Nickel specifically required for ureolysis and cannot be replaced by another metal, 0.5 mol of nickel is firmly bound to 1 mol of enzyme protein Pseudarthrobacter oxydans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.5 242000
-
 gel filtration Pseudarthrobacter oxydans

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.5 Pseudarthrobacter oxydans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.5
-
 Pseudarthrobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.5 urea + H2O
-
 Pseudarthrobacter oxydans CO2 + NH3
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.5 40
-
-
 Pseudarthrobacter oxydans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.5 65
-
 stable up to Pseudarthrobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.5 7.6
-
-
 Pseudarthrobacter oxydans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.5 5
-
 and below, nickel is irreversibly removed with concommitant loss of enzyme activity Pseudarthrobacter oxydans
3.5.1.5 7
-
 in presence of 10 mM EDTA protein-nickel binding remains intact Pseudarthrobacter oxydans