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Literature summary for 3.5.1.5 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
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Metals/Ions

Metals/Ions Comment Organism Structure
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
Nickel nickel metalloenzyme Klebsiella aerogenes

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Klebsiella aerogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
apoenzyme Klebsiella aerogenes

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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