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Literature summary extracted from

  • Lee, M.H.; Mulrooney, S.B.; Hausinger, R.P.
    Purification, characterization, and in vivo reconstitution of Klebsiella aerogenes urease apoenzyme (1990), J. Bacteriol., 172, 4427-4431.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.5 Nickel addition of Ni to purified apourease does not yield active enzyme, the apoenzyme is very slowly activated in vivo by addition of Ni2+ ions to Ni-free cell cultures, apourease activation is an energy-dependent process that is deactivated by cell disruption Klebsiella aerogenes
3.5.1.5 Nickel nickel metalloenzyme Klebsiella aerogenes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.5 9000
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE Klebsiella aerogenes
3.5.1.5 11000
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE Klebsiella aerogenes
3.5.1.5 72000
-
alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE Klebsiella aerogenes
3.5.1.5 224000
-
gel filtration Klebsiella aerogenes

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.5 Klebsiella aerogenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.5 apoenzyme Klebsiella aerogenes

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.5.1.5 decamer alpha2beta4tau4, 2 * 72000 + 4 * 11000 + 4 * 9000, SDS-PAGE Klebsiella aerogenes

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.5 additional information
-
Ni substantially increase stability of the intact metalloprotein, Tm = 79°C compared with apoenzyme Tm = 62°C Klebsiella aerogenes