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