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Literature summary for 3.5.1.5 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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Nickel nickel metalloenzyme Pseudarthrobacter oxydans
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]

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

Organism

Organism UniProt Comment Textmining
Pseudarthrobacter oxydans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudarthrobacter oxydans

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
Pseudarthrobacter oxydans

pH Stability

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