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Literature summary for 3.5.1.5 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)

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

Protein Variants

Protein Variants Comment Organism
D221A low activity, small increase in Km-value and pH 5 optimum Klebsiella aerogenes
H219A 1000fold increased Km-value over that of the native enzyme Klebsiella aerogenes
H219H 100fold increased Km-value over that of the native enzyme Klebsiella aerogenes
H219Q 100fold increased Km-value over that of the native enzyme Klebsiella aerogenes
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
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
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
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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Klebsiella aerogenes
-
-
-

Reaction

Reaction Comment Organism Reaction ID
urea + H2O = CO2 + 2 NH3 mechanism Klebsiella aerogenes

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

pH Optimum

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

pH Range

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