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Literature summary for 3.5.1.5 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
Search for more literature for 3.5.1.5

Inhibitors

Inhibitors Comment Organism Structure
Cd2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis
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
Ni2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis
Pb2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis
Zn2+ inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+ Canavalia ensiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
3.2
-
 Urea free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2 Canavalia ensiformis

Organism

Organism UniProt Comment Textmining
Canavalia ensiformis
-
 commercial preparation
-

Substrates and Products (Substrate)

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