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Literature summary for 3.5.1.5 extracted from

  • Quiroz-Valenzuela, S.; Sukuru, S.C.; Hausinger, R.P.; Kuhn, L.A.; Heller, W.T.
    The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering (2008), Arch. Biochem. Biophys., 480, 51-57.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Klebsiella aerogenes

Protein Variants

Protein Variants Comment Organism
G11P UreB, subunit beta, analysis of urease activation Klebsiella aerogenes
G18P UreB, subunit beta, analysis of urease activation Klebsiella aerogenes

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ urease activation: apoprotein (UreABC)3 + 6 Ni2+ Klebsiella aerogenes

Organism

Organism UniProt Comment Textmining
Klebsiella aerogenes P18314 and P18315 and P18316 subunits alpha, beta, gamma
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
440
-
G11P (UreB), 1.67 Ni2+/active site Klebsiella aerogenes
2200
-
wild type, 2.1 Ni2+/active site Klebsiella aerogenes

Subunits

Subunits Comment Organism
nonamer (UreABC)3 Klebsiella aerogenes

Synonyms

Synonyms Comment Organism
urease
-
Klebsiella aerogenes