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Literature summary extracted from

  • Godjevargova, T.; Gabrovska, K.
    Kinetic parameters of urease immobilized on modified acrylonitrile copolymer membranes in the presence and absence of Cu(II) ions (2005), Macromol. Biosci., 5, 459-466.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.5 Cd2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis
3.5.1.5 Cu2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+. Enzyme immobilized on membranes modified with NH2NH2/H2SO4, NaOH + ethylenediamine or H2O2 is most sensitive to Cu2+ Canavalia ensiformis
3.5.1.5 Ni2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis
3.5.1.5 Pb2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis
3.5.1.5 Zn2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.5 additional information
-
additional information kinetic analysis of enzyme immobilized on acrylonitrile copolymer membranes chemically modified by different methods. KM-value of enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2 is equal to that of free enzyme Canavalia ensiformis
3.5.1.5 3.2
-
Urea free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2 Canavalia ensiformis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.5 Canavalia ensiformis
-
commercial preparation
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.5 urea + H2O
-
Canavalia ensiformis CO2 + NH3
-
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