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Literature summary extracted from

  • Pearson, M.A.; Park, I.S.; Schaller, R.A.; Michel, L.O.; Karplus, P.A.; Hausinger, R.P.
    Kinetic and structural characterization of urease active site variants (2000), Biochemistry, 39, 8575-8574.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.5 wild-type and mutant enzyme Klebsiella aerogenes

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.5 D221A low activity, small increase in Km-value and pH 5 optimum Klebsiella aerogenes
3.5.1.5 H219A 1000fold increased Km-value over that of the native enzyme Klebsiella aerogenes
3.5.1.5 H219H 100fold increased Km-value over that of the native enzyme Klebsiella aerogenes
3.5.1.5 H219Q 100fold increased Km-value over that of the native enzyme Klebsiella aerogenes
3.5.1.5 H320A 100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9 Klebsiella aerogenes
3.5.1.5 H320N 100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9 Klebsiella aerogenes
3.5.1.5 H320Q 100000fold deficiencies in rates, modest Km changes, disorders in the peptide flap covering their active sites, the pH-optimum is anomalous with optima near pH 6 and shoulders that extend to pH 9 Klebsiella aerogenes
3.5.1.5 R336Q 0.0001fold decreased catalytic rate with near-normal pH dependence, unaffected Km-value, phenylglyoxal inactivates at over half the rate observed for the native enzyme Klebsiella aerogenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.5 2.4
-
 Urea wild-type enzyme Klebsiella aerogenes
3.5.1.5 2.7
-
 Urea mutant R336Q Klebsiella aerogenes
3.5.1.5 3.6
-
 Urea mutant D221N Klebsiella aerogenes
3.5.1.5 7.4
-
 Urea mutant H320N Klebsiella aerogenes
3.5.1.5 10.6
-
 Urea mutant H320Q Klebsiella aerogenes
3.5.1.5 10.9
-
 Urea mutant H320A Klebsiella aerogenes
3.5.1.5 24
-
 Urea mutant D221A Klebsiella aerogenes
3.5.1.5 175
-
 Urea mutant H219N Klebsiella aerogenes
3.5.1.5 227
-
 Urea mutant H219Q Klebsiella aerogenes
3.5.1.5 2090
-
 Urea mutant H219A Klebsiella aerogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.5 Nickel dinuclear nickel active site Klebsiella aerogenes

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.5 urea + H2O = CO2 + 2 NH3 mechanism Klebsiella aerogenes
a

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
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.5 0.06
-
 Urea mutant H320N Klebsiella aerogenes
3.5.1.5 0.068
-
 Urea mutant H320A Klebsiella aerogenes
3.5.1.5 0.33
-
 Urea mutant H320Q Klebsiella aerogenes
3.5.1.5 0.62
-
 Urea mutant R336Q Klebsiella aerogenes
3.5.1.5 1.7
-
 Urea mutant D221A Klebsiella aerogenes
3.5.1.5 60
-
 Urea mutant D221N Klebsiella aerogenes
3.5.1.5 194
-
 Urea mutant H219A Klebsiella aerogenes
3.5.1.5 322
-
 Urea mutant H219N Klebsiella aerogenes
3.5.1.5 1860
-
 Urea mutant H219Q Klebsiella aerogenes
3.5.1.5 2970
-
 Urea wild-type enzyme Klebsiella aerogenes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.5 5
-
 mutant D221A Klebsiella aerogenes
3.5.1.5 6
-
 mutant enzymes H320A, H320N and H320A Klebsiella aerogenes
3.5.1.5 8
-
 wild-type enzyme Klebsiella aerogenes

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.5 7 9 about 65% of maximal activity at pH 7.0 and 9.0 Klebsiella aerogenes